RRC ID 49533
Author Yano K, Niki H.
Title Multiple cis-Acting rDNAs Contribute to Nucleoid Separation and Recruit the Bacterial Condensin Smc-ScpAB.
Journal Cell Rep
Abstract Condensins load onto DNA to organize chromosomes. Smc-ScpAB clearly loads onto the parS sites bound by Spo0J, but other loading site(s) must operate independently of parS. In this study, we asked where and how Smc-ScpAB normally selects its loading site. Our results suggest that rDNA is also a loading site. A pull-down assay revealed that Smc-ScpAB preferentially loads onto rDNA in the wild-type cell and even in a Δspo0J mutant but not in a Δsmc mutant. Moreover, we showed that deletion mutants of rDNAs cause a defect in nucleoid separation, and at least two rDNAs near oriC are essential for separation. Full-length rDNA, including promoters, is required for loading and nucleoid separation. A synthetic defect by deletions of both rDNA and spo0J resulted in more aberrant nucleoid separation. We propose that a single-stranded segment of DNA that is exposed at highly transcribed rRNA operons would become a target for Smc-ScpAB loading.
Volume 21(5)
Pages 1347-1360
Published 2017-10-31
DOI 10.1016/j.celrep.2017.10.014
PII S2211-1247(17)31446-8
PMID 29091771
MeSH Adenosine Triphosphatases / genetics Adenosine Triphosphatases / metabolism* Bacillus subtilis / genetics Bacterial Proteins / genetics Bacterial Proteins / metabolism* Cell Cycle Proteins / genetics Cell Cycle Proteins / metabolism Cell Nucleolus / genetics Cell Nucleolus / metabolism DNA, Ribosomal / metabolism* DNA-Binding Proteins / genetics DNA-Binding Proteins / metabolism* Multiprotein Complexes / genetics Multiprotein Complexes / metabolism* Mutagenesis Plasmids / metabolism
IF 8.109
Times Cited 6
Altmetric score
オルトメトリクス指標項目
The most frequently cited source X(Twitter)
Total number of mentions 6
Altmetric score changes over past 6months 0.0
Resource
Prokaryotes B. subtilis MBS465 MBS466 MBS467 MBS468 MBS469 MBS470 MBS471 MBS472 MBS473 MBS474 MBS475 MBS476 MBS497 MBS498 MBS499 MBS500 MBS501 MBS502 MBS503 MBS504 MBS505 MBS506 MBS477 MBS507 MBS478 MBS479 MBS508 MBS480 MBS509 MBS481 MBS482 MBS510 MBS483 MBS511 MBS484 MBS485 MBS512 MBS486 MBS487 MBS513 MBS488 MBS489 MBS514 MBS515 MBS491 MBS516 MBS492 MBS517 MBS493 MBS518 MBS495 MBS496 MBS531 MBS532 MBS533 MBS534 MBP1 MBP2 MBS519 MBS520 MBS521 MBS522 MBS523 MBS524 MBS525 MBS526 MBS527 MBS528 MBS529 MBS530 MBP4 MBP3 MBP5 MBP6 MBP7 MBP8 MBP25 MBP9 MBP26 MBP27 MBP28 MBP10 MBP29 MBP11 MBP30 MBP12 MBP13 MBP14 MBP15 MBP16 MBP17 MBP18 MBP19 MBP20 MBP21 MBP22 MBP23 MBP24