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Double stranded RNA binding domain
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PDB id
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1stu
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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intracellular
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1 term
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Biochemical function
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RNA binding
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2 terms
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Embo J
14:3563-3571
(1995)
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PubMed id:
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NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5.
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M.Bycroft,
S.Grünert,
A.G.Murzin,
M.Proctor,
D.St Johnston.
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ABSTRACT
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The double-stranded RNA binding domain (dsRBD) is an approximately 65 amino acid
motif that is found in a variety of proteins that interact with double-stranded
(ds) RNA, such as Escherichia coli RNase III and the dsRNA-dependent kinase,
PKR. Drosophila staufen protein contains five copies of this motif, and the
third of these binds dsRNA in vitro. Using multinuclear/multidimensional NMR
methods, we have determined that staufen dsRBD3 forms a compact protein domain
with an alpha-beta-beta-beta-alpha structure in which the two alpha-helices lie
on one face of a three-stranded anti-parallel beta-sheet. This structure is very
similar to that of the N-terminal domain of a prokaryotic ribosomal protein S5.
Furthermore, the consensus derived from all known S5p family sequences shares
several conserved residues with the dsRBD consensus sequence, indicating that
the two domains share a common evolutionary origin. Using in vitro mutagenesis,
we have identified several surface residues which are important for the RNA
binding of the dsRBD, and these all lie on the same side of the domain. Two
residues that are essential for RNA binding, F32 and K50, are also conserved in
the S5 protein family, suggesting that the two domains interact with RNA in a
similar way.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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C.Dominguez,
M.Schubert,
O.Duss,
S.Ravindranathan,
and
F.H.Allain
(2011).
Structure determination and dynamics of protein-RNA complexes by NMR spectroscopy.
|
| |
Prog Nucl Magn Reson Spectrosc, 58,
1.
|
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|
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S.Yamashita,
T.Nagata,
M.Kawazoe,
C.Takemoto,
T.Kigawa,
P.Güntert,
N.Kobayashi,
T.Terada,
M.Shirouzu,
M.Wakiyama,
Y.Muto,
and
S.Yokoyama
(2011).
Structures of the first and second double-stranded RNA-binding domains of human TAR RNA-binding protein.
|
| |
Protein Sci, 20,
118-130.
|
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|
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C.Martel,
S.Dugré-Brisson,
K.Boulay,
B.Breton,
G.Lapointe,
S.Armando,
V.Trépanier,
T.Duchaîne,
M.Bouvier,
and
L.Desgroseillers
(2010).
Multimerization of Staufen1 in live cells.
|
| |
RNA, 16,
585-597.
|
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|
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J.P.Palavicini,
M.A.O'Connell,
and
J.J.Rosenthal
(2009).
An extra double-stranded RNA binding domain confers high activity to a squid RNA editing enzyme.
|
| |
RNA, 15,
1208-1218.
|
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|
|
|
|
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M.M.Mhlanga,
D.P.Bratu,
A.Genovesio,
A.Rybarska,
N.Chenouard,
U.Nehrbass,
and
J.C.Olivo-Marin
(2009).
In vivo colocalisation of oskar mRNA and trans-acting proteins revealed by quantitative imaging of the Drosophila oocyte.
|
| |
PLoS One, 4,
e6241.
|
 |
|
|
|
|
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M.Nowotny,
and
W.Yang
(2009).
Structural and functional modules in RNA interference.
|
| |
Curr Opin Struct Biol, 19,
286-293.
|
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|
|
|
|
 |
M.Nowotny,
S.M.Cerritelli,
R.Ghirlando,
S.A.Gaidamakov,
R.J.Crouch,
and
W.Yang
(2008).
Specific recognition of RNA/DNA hybrid and enhancement of human RNase H1 activity by HBD.
|
| |
EMBO J, 27,
1172-1181.
|
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|
PDB code:
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B.J.Fenner,
W.Goh,
and
J.Kwang
(2007).
Dissection of double-stranded RNA binding protein B2 from betanodavirus.
|
| |
J Virol, 81,
5449-5459.
|
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|
|
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|
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N.Okazaki,
M.Kumei,
M.Manzoku,
S.Kuramitsu,
M.Shirouzu,
A.Shinkai,
and
S.Yokoyama
(2007).
Structure of a UPF0150-family protein from Thermus thermophilus HB8.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun, 63,
173-177.
|
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PDB code:
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F.Li,
and
S.W.Ding
(2006).
Virus counterdefense: diverse strategies for evading the RNA-silencing immunity.
|
| |
Annu Rev Microbiol, 60,
503-531.
|
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|
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K.A.Chilibeck,
T.Wu,
C.Liang,
M.J.Schellenberg,
E.M.Gesner,
J.M.Lynch,
and
A.M.MacMillan
(2006).
FRET analysis of in vivo dimerization by RNA-editing enzymes.
|
| |
J Biol Chem, 281,
16530-16535.
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M.Hallegger,
A.Taschner,
and
M.F.Jantsch
(2006).
RNA aptamers binding the double-stranded RNA-binding domain.
|
| |
RNA, 12,
1993-2004.
|
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|
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A.K.Henras,
M.Sam,
S.L.Hiley,
H.Wu,
T.R.Hughes,
J.Feigon,
and
G.F.Chanfreau
(2005).
Biochemical and genomic analysis of substrate recognition by the double-stranded RNA binding domain of yeast RNase III.
|
| |
RNA, 11,
1225-1237.
|
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|
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K.Y.Chang,
and
A.Ramos
(2005).
The double-stranded RNA-binding motif, a versatile macromolecular docking platform.
|
| |
FEBS J, 272,
2109-2117.
|
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|
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P.A.Beal
(2005).
Duplex RNA-binding enzymes: headliners from neurobiology, virology, and development.
|
| |
Chembiochem, 6,
257-266.
|
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|
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P.O.Craig,
P.M.Berguer,
N.Ainciart,
V.Zylberman,
M.G.Thomas,
L.J.Martinez Tosar,
A.Bulloj,
G.L.Boccaccio,
and
F.A.Goldbaum
(2005).
Multiple display of a protein domain on a bacterial polymeric scaffold.
|
| |
Proteins, 61,
1089-1100.
|
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|
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Y.Chen,
and
G.Varani
(2005).
Protein families and RNA recognition.
|
| |
FEBS J, 272,
2088-2097.
|
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|
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B.Tian,
P.C.Bevilacqua,
A.Diegelman-Parente,
and
M.B.Mathews
(2004).
The double-stranded-RNA-binding motif: interference and much more.
|
| |
Nat Rev Mol Cell Biol, 5,
1013-1023.
|
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|
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H.Fan,
and
A.E.Mark
(2004).
Refinement of homology-based protein structures by molecular dynamics simulation techniques.
|
| |
Protein Sci, 13,
211-220.
|
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|
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H.Wu,
A.Henras,
G.Chanfreau,
and
J.Feigon
(2004).
Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III.
|
| |
Proc Natl Acad Sci U S A, 101,
8307-8312.
|
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PDB code:
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|
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J.Blaszczyk,
J.Gan,
J.E.Tropea,
D.L.Court,
D.S.Waugh,
and
X.Ji
(2004).
Noncatalytic assembly of ribonuclease III with double-stranded RNA.
|
| |
Structure, 12,
457-466.
|
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PDB codes:
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N.Leulliot,
S.Quevillon-Cheruel,
M.Graille,
H.van Tilbeurgh,
T.C.Leeper,
K.S.Godin,
T.E.Edwards,
S.T.Sigurdsson,
N.Rozenkrants,
R.J.Nagel,
M.Ares,
and
G.Varani
(2004).
A new alpha-helical extension promotes RNA binding by the dsRBD of Rnt1p RNAse III.
|
| |
EMBO J, 23,
2468-2477.
|
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PDB codes:
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P.Villacé,
R.M.Marión,
and
J.Ortín
(2004).
The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs.
|
| |
Nucleic Acids Res, 32,
2411-2420.
|
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|
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|
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A.Gallo,
L.P.Keegan,
G.M.Ring,
and
M.A.O'Connell
(2003).
An ADAR that edits transcripts encoding ion channel subunits functions as a dimer.
|
| |
EMBO J, 22,
3421-3430.
|
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|
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|
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C.B.Carlson,
O.M.Stephens,
and
P.A.Beal
(2003).
Recognition of double-stranded RNA by proteins and small molecules.
|
| |
Biopolymers, 70,
86.
|
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|
|
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|
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H.Fan,
and
A.E.Mark
(2003).
Relative stability of protein structures determined by X-ray crystallography or NMR spectroscopy: a molecular dynamics simulation study.
|
| |
Proteins, 53,
111-120.
|
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|
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|
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T.W.Reichman,
and
M.B.Mathews
(2003).
RNA binding and intramolecular interactions modulate the regulation of gene expression by nuclear factor 110.
|
| |
RNA, 9,
543-554.
|
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|
|
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|
 |
A.Strehblow,
M.Hallegger,
and
M.F.Jantsch
(2002).
Nucleocytoplasmic distribution of human RNA-editing enzyme ADAR1 is modulated by double-stranded RNA-binding domains, a leucine-rich export signal, and a putative dimerization domain.
|
| |
Mol Biol Cell, 13,
3822-3835.
|
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|
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|
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B.L.Bass
(2002).
RNA editing by adenosine deaminases that act on RNA.
|
| |
Annu Rev Biochem, 71,
817-846.
|
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|
|
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|
 |
D.Baltzis,
S.Li,
and
A.E.Koromilas
(2002).
Functional characterization of pkr gene products expressed in cells from mice with a targeted deletion of the N terminus or C terminus domain of PKR.
|
| |
J Biol Chem, 277,
38364-38372.
|
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|
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|
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K.Ye,
A.Serganov,
W.Hu,
M.Garber,
and
D.J.Patel
(2002).
Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold.
|
| |
Eur J Biochem, 269,
5182-5191.
|
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PDB code:
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T.Castrignanò,
G.Chillemi,
G.Varani,
and
A.Desideri
(2002).
Molecular dynamics simulation of the RNA complex of a double-stranded RNA-binding domain reveals dynamic features of the intermolecular interface and its hydration.
|
| |
Biophys J, 83,
3542-3552.
|
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|
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V.Anantharaman,
E.V.Koonin,
and
L.Aravind
(2002).
Comparative genomics and evolution of proteins involved in RNA metabolism.
|
| |
Nucleic Acids Res, 30,
1427-1464.
|
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|
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Y.Ben-Asouli,
Y.Banai,
Y.Pel-Or,
A.Shir,
and
R.Kaempfer
(2002).
Human interferon-gamma mRNA autoregulates its translation through a pseudoknot that activates the interferon-inducible protein kinase PKR.
|
| |
Cell, 108,
221-232.
|
 |
|
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|
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A.M.Olland,
J.Jané-Valbuena,
L.A.Schiff,
M.L.Nibert,
and
S.C.Harrison
(2001).
Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.
|
| |
EMBO J, 20,
979-989.
|
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PDB code:
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C.R.Eckmann,
A.Neunteufl,
L.Pfaffstetter,
and
M.F.Jantsch
(2001).
The human but not the Xenopus RNA-editing enzyme ADAR1 has an atypical nuclear localization signal and displays the characteristics of a shuttling protein.
|
| |
Mol Biol Cell, 12,
1911-1924.
|
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|
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|
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D.R.Taylor,
B.Tian,
P.R.Romano,
A.G.Hinnebusch,
M.M.Lai,
and
M.B.Mathews
(2001).
Hepatitis C virus envelope protein E2 does not inhibit PKR by simple competition with autophosphorylation sites in the RNA-binding domain.
|
| |
J Virol, 75,
1265-1273.
|
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|
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D.St Johnston
(2001).
The beginning of the end.
|
| |
EMBO J, 20,
6169-6179.
|
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|
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I.Lebars,
B.Lamontagne,
S.Yoshizawa,
S.Aboul-Elela,
and
D.Fourmy
(2001).
Solution structure of conserved AGNN tetraloops: insights into Rnt1p RNA processing.
|
| |
EMBO J, 20,
7250-7258.
|
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|
PDB codes:
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|
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I.M.Palacios,
and
D.St Johnston
(2001).
Getting the message across: the intracellular localization of mRNAs in higher eukaryotes.
|
| |
Annu Rev Cell Dev Biol, 17,
569-614.
|
 |
|
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|
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J.Blaszczyk,
J.E.Tropea,
M.Bubunenko,
K.M.Routzahn,
D.S.Waugh,
D.L.Court,
and
X.Ji
(2001).
Crystallographic and modeling studies of RNase III suggest a mechanism for double-stranded RNA cleavage.
|
| |
Structure, 9,
1225-1236.
|
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PDB codes:
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J.M.Pérez-Cañadillas,
and
G.Varani
(2001).
Recent advances in RNA-protein recognition.
|
| |
Curr Opin Struct Biol, 11,
53-58.
|
 |
|
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|
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K.Kurimoto,
S.Fukai,
O.Nureki,
Y.Muto,
and
S.Yokoyama
(2001).
Crystal structure of human AUH protein, a single-stranded RNA binding homolog of enoyl-CoA hydratase.
|
| |
Structure, 9,
1253-1263.
|
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|
PDB code:
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|
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K.M.Vattem,
K.A.Staschke,
S.Zhu,
and
R.C.Wek
(2001).
Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha).
|
| |
Eur J Biochem, 268,
1143-1153.
|
 |
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|
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L.Parsons,
E.Eisenstein,
and
J.Orban
(2001).
Solution structure of HI0257, a bacterial ribosome binding protein.
|
| |
Biochemistry, 40,
10979-10986.
|
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PDB code:
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|
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M.Monshausen,
U.Putz,
M.Rehbein,
M.Schweizer,
L.DesGroseillers,
D.Kuhl,
D.Richter,
and
S.Kindler
(2001).
Two rat brain staufen isoforms differentially bind RNA.
|
| |
J Neurochem, 76,
155-165.
|
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|
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N.V.Jammi,
and
P.A.Beal
(2001).
Phosphorylation of the RNA-dependent protein kinase regulates its RNA-binding activity.
|
| |
Nucleic Acids Res, 29,
3020-3029.
|
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|
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|
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R.J.Spanggord,
and
P.A.Beal
(2001).
Selective binding by the RNA binding domain of PKR revealed by affinity cleavage.
|
| |
Biochemistry, 40,
4272-4280.
|
 |
|
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|
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T.A.Brandt,
and
B.L.Jacobs
(2001).
Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model.
|
| |
J Virol, 75,
850-856.
|
 |
|
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|
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A.Ramos,
S.Grünert,
J.Adams,
D.R.Micklem,
M.R.Proctor,
S.Freund,
M.Bycroft,
D.St Johnston,
and
G.Varani
(2000).
RNA recognition by a Staufen double-stranded RNA-binding domain.
|
| |
EMBO J, 19,
997.
|
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|
PDB code:
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|
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B.Lamontagne,
A.Tremblay,
and
S.Abou Elela
(2000).
The N-terminal domain that distinguishes yeast from bacterial RNase III contains a dimerization signal required for efficient double-stranded RNA cleavage.
|
| |
Mol Cell Biol, 20,
1104-1115.
|
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|
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|
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D.R.Micklem,
J.Adams,
S.Grünert,
and
D.St Johnston
(2000).
Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation.
|
| |
EMBO J, 19,
1366-1377.
|
 |
|
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|
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F.Böhl,
C.Kruse,
A.Frank,
D.Ferring,
and
R.P.Jansen
(2000).
She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p.
|
| |
EMBO J, 19,
5514-5524.
|
 |
|
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|
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F.Brizard,
M.Luo,
and
L.Desgroseillers
(2000).
Genomic organization of the human and mouse stau genes.
|
| |
DNA Cell Biol, 19,
331-339.
|
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|
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I.Fierro-Monti,
and
M.B.Mathews
(2000).
Proteins binding to duplexed RNA: one motif, multiple functions.
|
| |
Trends Biochem Sci, 25,
241-246.
|
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|
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L.Daviet,
M.Erard,
D.Dorin,
M.Duarte,
C.Vaquero,
and
A.Gatignol
(2000).
Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif.
|
| |
Eur J Biochem, 267,
2419-2431.
|
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|
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M.Bonin,
J.Oberstrass,
N.Lukacs,
K.Ewert,
E.Oesterschulze,
R.Kassing,
and
W.Nellen
(2000).
Determination of preferential binding sites for anti-dsRNA antibodies on double-stranded RNA by scanning force microscopy.
|
| |
RNA, 6,
563-570.
|
 |
|
|
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|
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R.J.Spanggord,
and
P.A.Beal
(2000).
Site-specific modification and RNA crosslinking of the RNA-binding domain of PKR.
|
| |
Nucleic Acids Res, 28,
1899-1905.
|
 |
|
|
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|
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T.Duchaîne,
H.J.Wang,
M.Luo,
S.V.Steinberg,
I.R.Nabi,
and
L.DesGroseillers
(2000).
A novel murine Staufen isoform modulates the RNA content of Staufen complexes.
|
| |
Mol Cell Biol, 20,
5592-5601.
|
 |
|
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|
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X.Zheng,
and
P.C.Bevilacqua
(2000).
Straightening of bulged RNA by the double-stranded RNA-binding domain from the protein kinase PKR.
|
| |
Proc Natl Acad Sci U S A, 97,
14162-14167.
|
 |
|
|
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|
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Y.Liu,
M.Lei,
and
C.E.Samuel
(2000).
Chimeric double-stranded RNA-specific adenosine deaminase ADAR1 proteins reveal functional selectivity of double-stranded RNA-binding domains from ADAR1 and protein kinase PKR.
|
| |
Proc Natl Acad Sci U S A, 97,
12541-12546.
|
 |
|
|
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|
 |
A.Ramos,
P.Bayer,
and
G.Varani
(1999).
Determination of the structure of the RNA complex of a double-stranded RNA-binding domain from Drosophila Staufen protein.
|
| |
Biopolymers, 52,
181-196.
|
 |
|
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|
 |
A.W.Nicholson
(1999).
Function, mechanism and regulation of bacterial ribonucleases.
|
| |
FEMS Microbiol Rev, 23,
371-390.
|
 |
|
|
|
|
 |
C.M.Fletcher,
T.V.Pestova,
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EMBO J, 18,
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PDB code:
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D.Zhou,
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Pac1p, an RNase III homolog, is required for formation of the 3' end of U2 snRNA in Schizosaccharomyces pombe.
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RNA, 5,
1083-1098.
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K.Strub,
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The Alu domain homolog of the yeast signal recognition particle consists of an Srp14p homodimer and a yeast-specific RNA structure.
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RNA, 5,
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A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum.
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Mol Cell Biol, 19,
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RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids.
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RNA, 5,
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A.J.Schuldt,
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PDB code:
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M.Huenges,
C.Rölz,
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EMBO J, 17,
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PDB code:
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M.Kumar,
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Binding of the protein kinase PKR to RNAs with secondary structure defects: role of the tandem A-G mismatch and noncontiguous helixes.
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Biochemistry, 37,
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Mol Cell Biol, 18,
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A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs.
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Nucleic Acids Res, 26,
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Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.
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EMBO J, 17,
5458-5465.
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PDB code:
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S.Wu,
K.U.Kumar,
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Identification and requirement of three ribosome binding domains in dsRNA-dependent protein kinase (PKR).
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Biochemistry, 37,
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S.Zhu,
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Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control.
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J Biol Chem, 273,
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Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome.
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Xlrbpa, a double-stranded RNA-binding protein associated with ribosomes and heterogeneous nuclear RNPs.
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J Cell Biol, 138,
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The crystal structure of the signal recognition particle Alu RNA binding heterodimer, SRP9/14.
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EMBO J, 16,
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PDB code:
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D.Ferrandon,
I.Koch,
E.Westhof,
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RNA-RNA interaction is required for the formation of specific bicoid mRNA 3' UTR-STAUFEN ribonucleoprotein particles.
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EMBO J, 16,
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Curr Opin Genet Dev, 7,
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Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis.
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Nucleic Acids Res, 25,
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The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.
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| |
Cell, 88,
235-242.
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PDB code:
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|
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M.J.Clemens,
and
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The double-stranded RNA-dependent protein kinase PKR: structure and function.
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J Interferon Cytokine Res, 17,
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Identification of an RNA-binding-loop in the N-terminal region of signal-recognition-particle protein SRP19.
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The 1.85 A structure of vaccinia protein VP39: a bifunctional enzyme that participates in the modification of both mRNA ends.
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PDB code:
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A.G.Murzin
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Structural classification of proteins: new superfamilies.
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Structural evidence for specific S8-RNA and S8-protein interactions within the 30S ribosomal subunit: ribosomal protein S8 from Bacillus stearothermophilus at 1.9 A resolution.
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| |
Structure, 4,
1093-1104.
|
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PDB code:
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|
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C.K.Ho,
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Mutational analysis of the vaccinia virus E3 protein defines amino acid residues involved in E3 binding to double-stranded RNA.
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J Virol, 70,
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D.R.Taylor,
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Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR.
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Three-dimensional structure and stability of the KH domain: molecular insights into the fragile X syndrome.
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Cell, 85,
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PDB codes:
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|
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G.Rotondo,
and
D.Frendewey
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Purification and characterization of the Pac1 ribonuclease of Schizosaccharomyces pombe.
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Defining the enzyme binding domain of a ribonuclease III processing signal. Ethylation interference and hydroxyl radical footprinting using catalytically inactive RNase III mutants.
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Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties.
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PDB codes:
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|
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S.Maas,
T.Melcher,
A.Herb,
P.H.Seeburg,
W.Keller,
S.Krause,
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Structural requirements for RNA editing in glutamate receptor pre-mRNAs by recombinant double-stranded RNA adenosine deaminase.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
|
|