Difference between revisions of "ScpA"

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* '''Description:''' DNA segregation and condensation protein <br/><br/>
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* '''Description:''' part of the [[condensin]] complex, chromosomal origin condensation and segregation <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || DNA segregation and condensation protein  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || DNA segregation and condensation protein  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || maintenance of chromosome structure
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|style="background:#ABCDEF;" align="center"|'''Function''' || segregation of replication origins
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU23220 scpA]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU23220 scpA]
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===Phenotypes of a mutant ===
 
===Phenotypes of a mutant ===
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* essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed]
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* ''[[scpA]]'' mutants are not viable on complex medim that allow rapid growth, but they are viable under conditions of slow growth {{PubMed|24440399,24440393}}
  
 
=== Database entries ===
 
=== Database entries ===
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* '''Kinetic information:'''
 
* '''Kinetic information:'''
  
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* '''Domains:'''  
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* '''[[Domains]]:'''  
  
 
* '''Modification:'''
 
* '''Modification:'''
  
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* '''Cofactor(s):'''
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* '''[[Cofactors]]:'''
  
 
* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
 
* '''[[SubtInteract|Interactions]]:'''  
 
* '''[[SubtInteract|Interactions]]:'''  
 +
** part of the [[condensin]] complex {{PubMed|24440399,24440393}}
 
** present as stable monomer {{PubMed|22385855}}
 
** present as stable monomer {{PubMed|22385855}}
 
** [[ScpA]]-[[Smc]] {{PubMed|23353789,22385855,12100548}}
 
** [[ScpA]]-[[Smc]] {{PubMed|23353789,22385855,12100548}}
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* '''[[Localization]]:'''  
 
* '''[[Localization]]:'''  
 
** nucleoid (Multiple) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
 
** nucleoid (Multiple) [http://www.ncbi.nlm.nih.gov/sites/entrez/16479537 PubMed]
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** the ([[Smc]])2-[[ScpA]]-[[ScpB]] complex forms two bipolar assemblies on the chromosome, one in each cell half {{PubMed|23475963}}
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** the [[condensin]] ([[Smc]])2-[[ScpA]]-[[ScpB]] complex forms two bipolar assemblies on the chromosome, one in each cell half, localization depends on [[Spo0J]] {{PubMed|24440393,23475963}}
  
 
=== Database entries ===
 
=== Database entries ===
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== Original publications ==
 
== Original publications ==
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<pubmed>12100548,12421306,12065423,7934830, 16479537, 19450516 15009890 11948165 23353789 23475963 22385855</pubmed>
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<pubmed>12100548,12421306,12065423,7934830, 16479537, 19450516 15009890 11948165 23353789 23475963 22385855 24440399,24440393</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 15:28, 16 February 2014

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

Gene name scpA
Synonyms ypuG
Essential yes PubMed
Product DNA segregation and condensation protein
Function segregation of replication origins
Gene expression levels in SubtiExpress: scpA
Interactions involving this protein in SubtInteract: ScpA
MW, pI 29 kDa, 4.788
Gene length, protein length 753 bp, 251 aa
Immediate neighbours scpB, ypuF
Sequences Protein DNA DNA_with_flanks
Genetic context
YpuG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ScpA 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: BSU23220

Phenotypes of a mutant

  • essential PubMed
  • scpA 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: scpA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
    • 3ZGX (complex between the head domain of Smc (aa 1 - 219 and 983 - 1186) and the N-terminal winged-helix domain of ScpA) PubMed
    • 4I98 (complex between ScpA (aa 1-160)-ScpB (aa 1-183) PubMed
  • 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

Rodrigo Reyes-Lamothe, Emilien Nicolas, David J Sherratt
Chromosome replication and segregation in bacteria.
Annu Rev Genet: 2012, 46;121-43
[PubMed:22934648] [WorldCat.org] [DOI] (I p)

Justin S Lenhart, Jeremy W Schroeder, Brian W Walsh, Lyle A Simmons
DNA repair and genome maintenance in Bacillus subtilis.
Microbiol Mol Biol Rev: 2012, 76(3);530-64
[PubMed:22933559] [WorldCat.org] [DOI] (I p)


Original publications

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)

Etienne Dervyn, Marie-Françoise Noirot-Gros, Peggy Mervelet, Steven McGovern, S Dusko Ehrlich, Patrice Polard, Philippe Noirot
The bacterial condensin/cohesin-like protein complex acts in DNA repair and regulation of gene expression.
Mol Microbiol: 2004, 51(6);1629-40
[PubMed:15009890] [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)

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