Molecular mechanism of sequence-directed DNA loading and translocation by FtsK.
Molecular mechanism of sequence-directed DNA loading and translocation by FtsK.
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FTSK的序列指导DNA负载和易位的分子机制。
DOI:
10.1016/j.molcel.2008.05.027
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发表时间:
2008-08-22
期刊:
影响因子:
16
通讯作者:
Grainge, Ian
中科院分区:
文献类型:
--
作者:
Lowe, Jan;Ellonen, Antti;Allen, Mark D.;Atkinson, Claire;Sherratt, David J.;Grainge, Ian
Dimeric circular chromosomes, formed by recombination between monomer sisters, cannot be segregated to daughter cells at cell division. XerCD site-specific recombination at the Escherichia coli dif site converts these dimers to monomers in a reaction that requires the DNA translocase FtsK. Short DNA sequences, KOPS (GGGNAGGG), which are polarized toward dif in the chromosome, direct FtsK translocation. FtsK interacts with KOPS through a C-terminal winged helix domain γ. The crystal structure of three FtsKγ domains bound to 8 bp KOPS DNA demonstrates how three γ domains recognize KOPS. Using covalently linked dimers of FtsK, we infer that three γ domains per hexamer are sufficient to recognize KOPS and load FtsK and subsequently activate recombination at dif. During translocation, FtsK fails to recognize an inverted KOPS sequence. Therefore, we propose that KOPS act solely as a loading site for FtsK, resulting in a uni-directionally oriented hexameric motor upon DNA.
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影响因子:
3.5
作者:
Dorazi, R;Dewar, SJ
通讯作者:
Dewar, SJ
影响因子:
11.4
作者:
Grainge, Ian;Bregu, Migena;Sherratt, David J.
通讯作者:
Sherratt, David J.
影响因子:
3.6
作者:
Liu, NJL;Dutton, RJ;Pogliano, K
通讯作者:
Pogliano, K
DOI:
10.1107/s0907444998003254
发表时间:
1998-09-01
期刊:
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子:
--
作者:
Brunger, AT;Adams, PD;Warren, GL
通讯作者:
Warren, GL
影响因子:
3.6
作者:
Bigot, S;Corre, J;Barre, FX
通讯作者:
Barre, FX