Difference between revisions of "ScpB"

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(Original publications)
(Original publications)
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== Original publications ==
 
== Original publications ==
<pubmed>12100548,12065423,12421306,22385855, 16479537, 19450516 12897137 7934830 11948165  23353789 24440399,24440393 25071173, 25557547 25951515 26253537 23475963</pubmed>
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<pubmed>12100548,12065423,12421306,22385855, 16479537, 19450516 12897137 7934830 11948165  23353789 24440399,24440393 25071173, 25557547 25951515 26253537 23475963 26295962</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:53, 24 August 2015

  • Description: part of the condensin complex, chromosomal origin condensation and segregation

Gene name scpB
Synonyms ypuH
Essential yes PubMed
Product DNA segregation and condensation protein
Function segregation of replication origins
Gene expression levels in SubtiExpress: scpB
Interactions involving this protein in SubtInteract: ScpB
MW, pI 21 kDa, 4.25
Gene length, protein length 591 bp, 197 aa
Immediate neighbours ypuI, scpA
Sequences Protein DNA DNA_with_flanks
Genetic context
YpuH context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ScpB expression.png















Categories containing this gene/protein

DNA condensation/ segregation, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU23210

Phenotypes of a mutant

  • essential PubMed
  • scpB mutants are not viable on complex medim that allow rapid growth, but they are viable under conditions of slow growth PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: scpB family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original publications

Martial Marbouty, Antoine Le Gall, Diego I Cattoni, Axel Cournac, Alan Koh, Jean-Bernard Fiche, Julien Mozziconacci, Heath Murray, Romain Koszul, Marcelo Nollmann
Condensin- and Replication-Mediated Bacterial Chromosome Folding and Origin Condensation Revealed by Hi-C and Super-resolution Imaging.
Mol Cell: 2015, 59(4);588-602
[PubMed:26295962] [WorldCat.org] [DOI] (I p)

Xindan Wang, Tung B K Le, Bryan R Lajoie, Job Dekker, Michael T Laub, David Z Rudner
Condensin promotes the juxtaposition of DNA flanking its loading site in Bacillus subtilis.
Genes Dev: 2015, 29(15);1661-75
[PubMed:26253537] [WorldCat.org] [DOI] (I p)

Larissa Wilhelm, Frank Bürmann, Anita Minnen, Ho-Chul Shin, Christopher P Toseland, Byung-Ha Oh, Stephan Gruber
SMC condensin entraps chromosomal DNA by an ATP hydrolysis dependent loading mechanism in Bacillus subtilis.
Elife: 2015, 4;
[PubMed:25951515] [WorldCat.org] [DOI] (I e)

Young-Min Soh, Frank Bürmann, Ho-Chul Shin, Takashi Oda, Kyeong Sik Jin, Christopher P Toseland, Cheolhee Kim, Hansol Lee, Soo Jin Kim, Min-Seok Kong, Marie-Laure Durand-Diebold, Yeon-Gil Kim, Ho Min Kim, Nam Ki Lee, Mamoru Sato, Byung-Ha Oh, Stephan Gruber
Molecular basis for SMC rod formation and its dissolution upon DNA binding.
Mol Cell: 2015, 57(2);290-303
[PubMed:25557547] [WorldCat.org] [DOI] (I p)

Xindan Wang, Paula Montero Llopis, David Z Rudner
Bacillus subtilis chromosome organization oscillates between two distinct patterns.
Proc Natl Acad Sci U S A: 2014, 111(35);12877-82
[PubMed:25071173] [WorldCat.org] [DOI] (I p)

Stephan Gruber, Jan-Willem Veening, Juri Bach, Martin Blettinger, Marc Bramkamp, Jeff Errington
Interlinked sister chromosomes arise in the absence of condensin during fast replication in B. subtilis.
Curr Biol: 2014, 24(3);293-8
[PubMed:24440399] [WorldCat.org] [DOI] (I p)

Xindan Wang, Olive W Tang, Eammon P Riley, David Z Rudner
The SMC condensin complex is required for origin segregation in Bacillus subtilis.
Curr Biol: 2014, 24(3);287-92
[PubMed:24440393] [WorldCat.org] [DOI] (I p)

Luise A K Kleine Borgmann, Hanna Hummel, Maximilian H Ulbrich, Peter L Graumann
SMC condensation centers in Bacillus subtilis are dynamic structures.
J Bacteriol: 2013, 195(10);2136-45
[PubMed:23475963] [WorldCat.org] [DOI] (I p)

Frank Bürmann, Ho-Chul Shin, Jérôme Basquin, Young-Min Soh, Victor Giménez-Oya, Yeon-Gil Kim, Byung-Ha Oh, Stephan Gruber
An asymmetric SMC-kleisin bridge in prokaryotic condensin.
Nat Struct Mol Biol: 2013, 20(3);371-9
[PubMed:23353789] [WorldCat.org] [DOI] (I p)

M E Fuentes-Perez, E J Gwynn, M S Dillingham, F Moreno-Herrero
Using DNA as a fiducial marker to study SMC complex interactions with the atomic force microscope.
Biophys J: 2012, 102(4);839-48
[PubMed:22385855] [WorldCat.org] [DOI] (I p)

Stephan Gruber, Jeff Errington
Recruitment of condensin to replication origin regions by ParB/SpoOJ promotes chromosome segregation in B. subtilis.
Cell: 2009, 137(4);685-96
[PubMed:19450516] [WorldCat.org] [DOI] (I p)

Jean-Christophe Meile, Ling Juan Wu, S Dusko Ehrlich, Jeff Errington, Philippe Noirot
Systematic localisation of proteins fused to the green fluorescent protein in Bacillus subtilis: identification of new proteins at the DNA replication factory.
Proteomics: 2006, 6(7);2135-46
[PubMed:16479537] [WorldCat.org] [DOI] (P p)

A Volkov, J Mascarenhas, C Andrei-Selmer, H D Ulrich, P L Graumann
A prokaryotic condensin/cohesin-like complex can actively compact chromosomes from a single position on the nucleoid and binds to DNA as a ring-like structure.
Mol Cell Biol: 2003, 23(16);5638-50
[PubMed:12897137] [WorldCat.org] [DOI] (P p)

Janet C Lindow, Masayoshi Kuwano, Shigeki Moriya, Alan D Grossman
Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein.
Mol Microbiol: 2002, 46(4);997-1009
[PubMed:12421306] [WorldCat.org] [DOI] (P p)

Jörg Soppa, Kazuo Kobayashi, Marie-Françoise Noirot-Gros, Dieter Oesterhelt, S Dusko Ehrlich, Etienne Dervyn, Naotake Ogasawara, Shigeki Moriya
Discovery of two novel families of proteins that are proposed to interact with prokaryotic SMC proteins, and characterization of the Bacillus subtilis family members ScpA and ScpB.
Mol Microbiol: 2002, 45(1);59-71
[PubMed:12100548] [WorldCat.org] [DOI] (P p)

Judita Mascarenhas, Jörg Soppa, Alexander V Strunnikov, Peter L Graumann
Cell cycle-dependent localization of two novel prokaryotic chromosome segregation and condensation proteins in Bacillus subtilis that interact with SMC protein.
EMBO J: 2002, 21(12);3108-18
[PubMed:12065423] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [WorldCat.org] [DOI] (P p)

V Azevedo, A Sorokin, S D Ehrlich, P Serror
The transcriptional organization of the Bacillus subtilis 168 chromosome region between the spoVAF and serA genetic loci.
Mol Microbiol: 1993, 10(2);397-405
[PubMed:7934830] [WorldCat.org] [DOI] (P p)