XerD unloads bacterial SMC complexes at the replication terminus.
XerD unloads bacterial SMC complexes at the replication terminus.
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DOI:
10.1016/j.molcel.2020.12.027
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发表时间:
2021-02-18
期刊:
影响因子:
16
通讯作者:
Wang X
中科院分区:
文献类型:
--
作者:
Karaboja X;Ren Z;Brandão HB;Paul P;Rudner DZ;Wang X
Bacillus subtilis structural maintenance of chromosomes (SMC) complexes are topologically loaded at centromeric sites adjacent to the replication origin by the partitioning protein ParB. These ring-shaped ATPases then translocate down the left and right chromosome arms while tethering them together. Here, we show that the site-specific recombinase XerD, which resolves chromosome dimers, is required to unload SMC tethers when they reach the terminus. We identify XerD-specific binding sites in the terminus region and show that they dictate the site of unloading in a manner that depends on XerD but not its catalytic residue, its partner protein XerC, or the recombination site dif. Finally, we provide evidence that ParB and XerD homologs perform similar functions in Staphylococcus aureus. Thus, two broadly conserved factors that act at the origin and terminus have second functions in loading and unloading SMC complexes that travel between them. SMC condensin complexes are loaded at replication origins by the partitioning protein ParB. Karaboja et al. show that condensins are unloaded when they reach the terminus by the recombinase XerD. Thus, broadly conserved factors that act at the origin and terminus load and unload SMC complexes that travel between them.
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DOI:
10.1126/science.aar7831
发表时间:
2018-04-06
期刊:
Science (New York, N.Y.)
影响因子:
--
作者:
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通讯作者:
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影响因子:
3.6
作者:
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通讯作者:
Grossman AD
DOI:
10.1146/annurev-cellbio-100814-125211
发表时间:
2015
影响因子:
11.3
作者:
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通讯作者:
Laub MT
影响因子:
64.8
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影响因子:
11.4
作者:
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通讯作者:
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