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Structural protein
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PDB id
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2ooe
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Contents |
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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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2 terms
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Biological process
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RNA processing
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2 terms
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Biochemical function
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binding
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1 term
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DOI no:
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Mol Cell
25:863-875
(2007)
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PubMed id:
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Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursors.
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Y.Bai,
T.C.Auperin,
C.Y.Chou,
G.G.Chang,
J.L.Manley,
L.Tong.
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ABSTRACT
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Cleavage stimulation factor (CstF) is a heterotrimeric protein complex essential
for polyadenylation of mRNA precursors. The 77 kDa subunit, CstF-77, is known to
mediate interactions with the other two subunits of CstF as well as with other
components of the polyadenylation machinery. We report here the crystal
structure of the HAT (half a TPR) domain of murine CstF-77, as well as its
C-terminal subdomain. Structural and biochemical studies show that the HAT
domain consists of two subdomains, HAT-N and HAT-C domains, with drastically
different orientations of their helical motifs. The structures reveal a highly
elongated dimer, spanning 165 A, with the dimerization mediated by the HAT-C
domain. Light-scattering studies, yeast two-hybrid assays, and analytical
ultracentrifugation measurements confirm this self-association. The mode of
dimerization and the relative arrangement of the HAT-N and HAT-C domains are
unique to CstF-77. Our data support a role for CstF dimerization in pre-mRNA 3'
end processing.
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Selected figure(s)
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Figure 1.
Figure 1. Sequence Alignment of CstF-77
(A) Schematic
drawing of the domain organization of murine CstF-77. The HAT
motifs are shown in yellow and labeled. The segment near the end
of the HAT-N domain is shown in cyan, and that near the end of
the HAT-C domain is shown in green. The proline-rich segment is
shown in gray. The ^* and + symbols indicate the conserved
tryptophan and tyrosine residues in each HAT repeat,
respectively.
(B) Sequence alignment of murine CstF-77,
Drosophila Suppressor of forked (Su[f]), and yeast Rna14. The
secondary structure elements (S.S.) are labeled. Residues shown
in magenta are in the dimer interface of the HAT domain.
Residues missing in the current model of CstF-77 are shown in
italic.
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Figure 2.
Figure 2. Structure of the HAT-C Domain of Murine CstF-77
(A) Stereo drawing of the structure of the HAT-C domain
dimer. One monomer is shown in yellow, and the other is shown in
cyan. The HAT motifs are labeled, and the magenta oval indicates
the two-fold axis of the dimer.
(B) Structure of the HAT-C
domain dimer, after 90° rotation around the vertical axis
from (A).
(C) Stereo drawing showing detailed interactions
in the dimer interface of the HAT-C domain. Side chains for
residues contributing >40 Å^2 of surface area to the dimer
interface are shown in green and magenta for the two monomers,
respectively.
(D) Molecular surface of the HAT-C domain
dimer, colored based on electrostatic potential. The C termini
of the two monomers are labeled, located at the rim of the
pocket. (A)–(C) are produced with Ribbons (Carson, 1987), and
(D) is produced with Grasp (Nicholls et al., 1991).
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2007,
25,
863-875)
copyright 2007.
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Figures were
selected
by an automated process.
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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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M.Moreno-Morcillo,
L.Minvielle-Sébastia,
S.Fribourg,
and
C.D.Mackereth
(2011).
Locked tether formation by cooperative folding of Rna14p monkeytail and Rna15p hinge domains in the yeast CF IA complex.
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Structure, 19,
534-545.
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PDB code:
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B.M.Lunde,
S.L.Reichow,
M.Kim,
H.Suh,
T.C.Leeper,
F.Yang,
H.Mutschler,
S.Buratowski,
A.Meinhart,
and
G.Varani
(2010).
Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.
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Nat Struct Mol Biol, 17,
1195-1201.
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PDB codes:
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C.Pancevac,
D.C.Goldstone,
A.Ramos,
and
I.A.Taylor
(2010).
Structure of the Rna15 RRM-RNA complex reveals the molecular basis of GU specificity in transcriptional 3'-end processing factors.
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Nucleic Acids Res, 38,
3119-3132.
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PDB codes:
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F.Liu,
S.Marquardt,
C.Lister,
S.Swiezewski,
and
C.Dean
(2010).
Targeted 3' processing of antisense transcripts triggers Arabidopsis FLC chromatin silencing.
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Science, 327,
94-97.
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J.A.Hockert,
H.J.Yeh,
and
C.C.MacDonald
(2010).
The hinge domain of the cleavage stimulation factor protein CstF-64 is essential for CstF-77 interaction, nuclear localization, and polyadenylation.
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J Biol Chem, 285,
695-704.
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S.C.Cheng,
G.G.Chang,
and
C.Y.Chou
(2010).
Mutation of Glu-166 blocks the substrate-induced dimerization of SARS coronavirus main protease.
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Biophys J, 98,
1327-1336.
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E.A.Champion,
L.Kundrat,
L.Regan,
and
S.J.Baserga
(2009).
A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics.
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Protein Eng Des Sel, 22,
431-439.
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G.A.Palidwor,
S.Shcherbinin,
M.R.Huska,
T.Rasko,
U.Stelzl,
A.Arumughan,
R.Foulle,
P.Porras,
L.Sanchez-Pulido,
E.E.Wanker,
and
M.A.Andrade-Navarro
(2009).
Detection of alpha-rod protein repeats using a neural network and application to huntingtin.
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PLoS Comput Biol, 5,
e1000304.
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G.S.Shankarling,
P.W.Coates,
B.Dass,
and
C.C.Macdonald
(2009).
A family of splice variants of CstF-64 expressed in vertebrate nervous systems.
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BMC Mol Biol, 10,
22.
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S.A.Kennedy,
M.L.Frazier,
M.Steiniger,
A.M.Mast,
W.F.Marzluff,
and
M.R.Redinbo
(2009).
Crystal structure of the HEAT domain from the Pre-mRNA processing factor Symplekin.
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J Mol Biol, 392,
115-128.
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PDB code:
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Y.Shi,
D.C.Di Giammartino,
D.Taylor,
A.Sarkeshik,
W.J.Rice,
J.R.Yates,
J.Frank,
and
J.L.Manley
(2009).
Molecular architecture of the human pre-mRNA 3' processing complex.
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Mol Cell, 33,
365-376.
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C.Mueller-Dieckmann,
S.Kernstock,
J.Mueller-Dieckmann,
M.S.Weiss,
and
F.Koch-Nolte
(2008).
Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 64,
156-162.
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PDB code:
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C.R.Mandel,
Y.Bai,
and
L.Tong
(2008).
Protein factors in pre-mRNA 3'-end processing.
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| |
Cell Mol Life Sci, 65,
1099-1122.
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E.A.Champion,
B.H.Lane,
M.E.Jackrel,
L.Regan,
and
S.J.Baserga
(2008).
A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21 is essential for efficient pre-rRNA processing.
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| |
Mol Cell Biol, 28,
6547-6556.
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|
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K.Ryan,
and
D.L.Bauer
(2008).
Finishing touches: post-translational modification of protein factors involved in mammalian pre-mRNA 3' end formation.
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| |
Int J Biochem Cell Biol, 40,
2384-2396.
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|
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P.Legrand,
N.Pinaud,
L.Minvielle-Sébastia,
and
S.Fribourg
(2007).
The structure of the CstF-77 homodimer provides insights into CstF assembly.
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| |
Nucleic Acids Res, 35,
4515-4522.
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PDB code:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
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.
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Links
