Difference between revisions of "Smc"
| Line 1: | Line 1: | ||
| − | * '''Description:''' | + | * '''Description:''' part of the [[condensin]] complex, chromosomal origin condensation and segregation SMC protein <br/><br/> |
{| align="right" border="1" cellpadding="2" | {| align="right" border="1" cellpadding="2" | ||
| Line 12: | Line 12: | ||
|style="background:#ABCDEF;" align="center"| '''Product''' || chromosome condensation and segregation SMC protein | |style="background:#ABCDEF;" align="center"| '''Product''' || chromosome condensation and segregation SMC protein | ||
|- | |- | ||
| − | |style="background:#ABCDEF;" align="center"|'''Function''' || | + | |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=BSU15940 smc] | |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=BSU15940 smc] | ||
| Line 57: | Line 57: | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| − | + | * essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] | |
| − | essential [http://www.ncbi.nlm.nih.gov/pubmed/12682299 PubMed] | + | * ''[[smc]]'' 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 === | ||
| Line 82: | Line 82: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| + | ** part of the [[condensin]] complex {{PubMed|24440399,24440393}} | ||
** forms dimers {{PubMed|22385855}} | ** forms dimers {{PubMed|22385855}} | ||
** [[ScpA]]-[[Smc]] {{PubMed|12100548}} | ** [[ScpA]]-[[Smc]] {{PubMed|12100548}} | ||
| Line 98: | Line 99: | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
** nucleoid (heterogeneous) {{PubMed|16479537}} | ** nucleoid (heterogeneous) {{PubMed|16479537}} | ||
| − | ** the ([[Smc]])2-[[ScpA]]-[[ScpB]] complex forms two bipolar assemblies on the chromosome, one in each cell half {{PubMed|23475963}} | + | ** 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 === | ||
| Line 151: | Line 152: | ||
==Original publications== | ==Original publications== | ||
| − | <pubmed>9791128,12100548,17416649,19450516,12421306,11395470, 19450517, 19450516 15009890 16479537 21630458 23353789 22385855 23475963</pubmed> | + | <pubmed>9791128,12100548,17416649,19450516,12421306,11395470, 19450517, 19450516 15009890 16479537 21630458 23353789 22385855 24440399,24440393 23475963</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 SMC protein
| Gene name | smc |
| Synonyms | ylqA |
| Essential | yes PubMed |
| Product | chromosome condensation and segregation SMC protein |
| Function | segregation of replication origins |
| Gene expression levels in SubtiExpress: smc | |
| Interactions involving this protein in SubtInteract: Smc | |
| Metabolic function and regulation of this protein in SubtiPathways: Protein secretion | |
| MW, pI | 135 kDa, 5.266 |
| Gene length, protein length | 3558 bp, 1186 aa |
| Immediate neighbours | rnc, ftsY |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
DNA condensation/ segregation, essential genes
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15940
Phenotypes of a mutant
- essential PubMed
- smc 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: SMC family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P51834
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
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)
Elodie Marchadier, Rut Carballido-López, Sophie Brinster, Céline Fabret, Peggy Mervelet, Philippe Bessières, Marie-Françoise Noirot-Gros, Vincent Fromion, Philippe Noirot
An expanded protein-protein interaction network in Bacillus subtilis reveals a group of hubs: Exploration by an integrative approach.
Proteomics: 2011, 11(15);2981-91
[PubMed:21630458]
[WorldCat.org]
[DOI]
(I p)
Nora L Sullivan, Kathleen A Marquis, David Z Rudner
Recruitment of SMC by ParB-parS organizes the origin region and promotes efficient chromosome segregation.
Cell: 2009, 137(4);697-707
[PubMed:19450517]
[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)
Robert A Britton, Elke Küster-Schöck, Thomas A Auchtung, Alan D Grossman
SOS induction in a subpopulation of structural maintenance of chromosome (Smc) mutant cells in Bacillus subtilis.
J Bacteriol: 2007, 189(12);4359-66
[PubMed:17416649]
[WorldCat.org]
[DOI]
(P 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)
P L Graumann, R Losick
Coupling of asymmetric division to polar placement of replication origin regions in Bacillus subtilis.
J Bacteriol: 2001, 183(13);4052-60
[PubMed:11395470]
[WorldCat.org]
[DOI]
(P p)
P L Graumann, R Losick, A V Strunnikov
Subcellular localization of Bacillus subtilis SMC, a protein involved in chromosome condensation and segregation.
J Bacteriol: 1998, 180(21);5749-55
[PubMed:9791128]
[WorldCat.org]
[DOI]
(P p)
