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PDBsum entry 1i1v
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Deoxyribonucleic acid
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PDB id
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1i1v
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DOI no:
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Proc Natl Acad Sci U S A
95:11071-11076
(1998)
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PubMed id:
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Base pair switching by interconversion of sugar puckers in DNA extended by proteins of RecA-family: a model for homology search in homologous genetic recombination.
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T.Nishinaka,
A.Shinohara,
Y.Ito,
S.Yokoyama,
T.Shibata.
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ABSTRACT
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Escherichia coli RecA is a representative of proteins from the RecA family,
which promote homologous pairing and strand exchange between double-stranded DNA
and single-stranded DNA. These reactions are essential for homologous genetic
recombination in various organisms. From NMR studies, we previously reported a
novel deoxyribose-base stacking interaction between adjacent residues on the
extended single-stranded DNA bound to RecA protein. In this study, we found that
the same DNA structure was induced by the binding to Saccharomyces cerevisiae
Rad51 protein, indicating that the unique DNA structure induced by the binding
to RecA-homologs was conserved from prokaryotes to eukaryotes. On the basis of
this structure, we have formulated the structure of duplex DNA within filaments
formed by RecA protein and its homologs. Two types of molecular structures are
presented. One is the duplex structure that has the N-type sugar pucker. Its
helical pitch is approximately 95 A (18.6 bp/turn), corresponding to that of an
active, or ATP-form of the RecA filament. The other is one that has the S-type
sugar pucker. Its helical pitch is approximately 64 A (12.5 bp/turn),
corresponding to that of an inactive, or ADP-form of the RecA filament. During
this modeling, we found that the interconversion of sugar puckers between the
N-type and the S-type rotates bases horizontally, while maintaining the
deoxyribose-base stacking interaction. We propose that this base rotation
enables base pair switching between double-stranded DNA and single-stranded DNA
to take place, facilitating homologous pairing and strand exchange. A possible
mechanism for strand exchange involving DNA rotation also is discussed.
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Selected figure(s)
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Figure 3.
Fig. 3. Base rotation by interconversion of sugar
puckers. (a) Top view of the base rotation caused by
interconversion of the sugar puckers. The sugar pucker of the
5'-residue (T, top) is in the S-type (Left) and the N-type
(Right), whereas that of the 3'-residue (A, bottom) is fixed in
the S-type. Note that the hydrogen-bonding vector is rotated
toward its major groove by the conversion from the S-type to the
N-type. (b) Two types of deoxyribose-base stacking. All residues
are in the S-type sugar pucker (Left) or the N-type (Right)
sugar pucker.
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Figure 4.
Fig. 4. A three-stranded DNA model for homology search
and strand exchange considering the N-S interconversion of sugar
puckers. (a) A molecular model of base pair switch between
single- and double-stranded DNA. The bottom three residues are
in the N-type and the top three residues are in the S-type. Note
that the base pairing is altered by the conversion of sugar
puckers between the N- and S-type. (b) Base rotation schemes for
base pair switching against the interconversion of the sugar
puckers. The bases are rotated toward the minor groove when the
sugar puckers are converted from the N-type (Left) to the S-type
(Right) and toward the major groove with the opposite (S-type to
N-type) conversion.
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Figures were
selected
by the author.
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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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J.Miné-Hattab,
G.Fleury,
C.Prevost,
M.Dutreix,
and
J.L.Viovy
(2011).
Optimizing the design of oligonucleotides for homology directed gene targeting.
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PLoS One,
6,
e14795.
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F.Ling,
M.Yoshida,
and
T.Shibata
(2009).
Heteroduplex joint formation free of net topological change by Mhr1, a mitochondrial recombinase.
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J Biol Chem,
284,
9341-9353.
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T.Masuda,
Y.Ito,
T.Terada,
T.Shibata,
and
T.Mikawa
(2009).
A non-canonical DNA structure enables homologous recombination in various genetic systems.
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J Biol Chem,
284,
30230-30239.
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PDB codes:
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G.Lahoud,
K.Arar,
Y.M.Hou,
and
H.Gamper
(2008).
RecA-mediated strand invasion of DNA by oligonucleotides substituted with 2-aminoadenine and 2-thiothymine.
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Nucleic Acids Res,
36,
6806-6815.
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N.Mazloum,
Q.Zhou,
and
W.K.Holloman
(2007).
DNA binding, annealing, and strand exchange activities of Brh2 protein from Ustilago maydis.
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Biochemistry,
46,
7163-7173.
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A.Kegel,
P.Martinez,
S.D.Carter,
and
S.U.Aström
(2006).
Genome wide distribution of illegitimate recombination events in Kluyveromyces lactis.
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Nucleic Acids Res,
34,
1633-1645.
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J.Xiao,
A.M.Lee,
and
S.F.Singleton
(2006).
Direct evaluation of a kinetic model for RecA-mediated DNA-strand exchange: the importance of nucleic acid dynamics and entropy during homologous genetic recombination.
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Chembiochem,
7,
1265-1278.
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M.Petukhov,
D.Lebedev,
V.Shalguev,
A.Islamov,
A.Kuklin,
V.Lanzov,
and
V.Isaev-Ivanov
(2006).
Conformational flexibility of RecA protein filament: transitions between compressed and stretched states.
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Proteins,
65,
296-304.
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R.Fulconis,
M.Dutreix,
and
J.L.Viovy
(2005).
Numerical investigation of sequence dependence in homologous recognition: evidence for homology traps.
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Biophys J,
88,
3770-3779.
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A.K.Shchyolkina,
D.N.Kaluzhny,
O.F.Borisova,
M.E.Hawkins,
R.L.Jernigan,
T.M.Jovin,
D.J.Arndt-Jovin,
and
V.B.Zhurkin
(2004).
Formation of an intramolecular triple-stranded DNA structure monitored by fluorescence of 2-aminopurine or 6-methylisoxanthopterin.
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Nucleic Acids Res,
32,
432-440.
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B.Bi,
N.Rybalchenko,
E.I.Golub,
and
C.M.Radding
(2004).
Human and yeast Rad52 proteins promote DNA strand exchange.
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Proc Natl Acad Sci U S A,
101,
9568-9572.
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E.Folta-Stogniew,
S.O'Malley,
R.Gupta,
K.S.Anderson,
and
C.M.Radding
(2004).
Exchange of DNA base pairs that coincides with recognition of homology promoted by E. coli RecA protein.
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Mol Cell,
15,
965-975.
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K.D.Dorfman,
R.Fulconis,
M.Dutreix,
and
J.L.Viovy
(2004).
Model of RecA-mediated homologous recognition.
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Phys Rev Lett,
93,
268102.
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K.Klapstein,
T.Chou,
and
R.Bruinsma
(2004).
Physics of RecA-mediated homologous recognition.
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Biophys J,
87,
1466-1477.
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P.Noirot,
R.C.Gupta,
C.M.Radding,
and
R.D.Kolodner
(2003).
Hallmarks of homology recognition by RecA-like recombinases are exhibited by the unrelated Escherichia coli RecT protein.
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EMBO J,
22,
324-334.
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M.Frank-Vaillant,
and
S.Marcand
(2002).
Transient stability of DNA ends allows nonhomologous end joining to precede homologous recombination.
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Mol Cell,
10,
1189-1199.
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S.J.Shi,
A.Scheffer,
E.Bjeldanes,
M.A.Reynolds,
and
L.J.Arnold
(2001).
DNA exhibits multi-stranded binding recognition on glass microarrays.
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Nucleic Acids Res,
29,
4251-4256.
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T.Shibata,
T.Nishinaka,
T.Mikawa,
H.Aihara,
H.Kurumizaka,
S.Yokoyama,
and
Y.Ito
(2001).
Homologous genetic recombination as an intrinsic dynamic property of a DNA structure induced by RecA/Rad51-family proteins: a possible advantage of DNA over RNA as genomic material.
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Proc Natl Acad Sci U S A,
98,
8425-8432.
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H.B.Gamper,
Y.M.Hou,
and
E.B.Kmiec
(2000).
Evidence for a four-strand exchange catalyzed by the RecA protein.
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Biochemistry,
39,
15272-15281.
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H.Zhou,
Y.Zhang,
and
Z.Ou-Yang
(2000).
Elastic property of single double-stranded DNA molecules: theoretical study and comparison with experiments.
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Phys Rev E Stat Phys Plasmas Fluids Relat Interdiscip Topics,
62,
1045-1058.
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K.P.Rice,
J.C.Chaput,
M.M.Cox,
and
C.Switzer
(2000).
RecA protein promotes strand exchange with DNA substrates containing isoguanine and 5-methyl isocytosine.
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Biochemistry,
39,
10177-10188.
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S.Sen,
G.Karthikeyan,
and
B.J.Rao
(2000).
RecA realigns suboptimally paired frames of DNA repeats through a process that requires ATP hydrolysis.
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Biochemistry,
39,
10196-10206.
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F.Pâques,
and
J.E.Haber
(1999).
Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae.
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Microbiol Mol Biol Rev,
63,
349-404.
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G.Bertucat,
R.Lavery,
and
C.Prévost
(1999).
A molecular model for RecA-promoted strand exchange via parallel triple-stranded helices.
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Biophys J,
77,
1562-1576.
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J.E.Haber
(1999).
DNA recombination: the replication connection.
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Trends Biochem Sci,
24,
271-275.
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R.C.Gupta,
E.Folta-Stogniew,
S.O'Malley,
M.Takahashi,
and
C.M.Radding
(1999).
Rapid exchange of A:T base pairs is essential for recognition of DNA homology by human Rad51 recombination protein.
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Mol Cell,
4,
705-714.
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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
codes are
shown on the right.
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}
}
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