Difference between revisions of "YhaM"

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=References=
 
=References=
  
<pubmed> 19553197, 16267290, 16479537,17981983, 15805522 19880604 </pubmed>
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<pubmed>     12399495 19553197, 16267290, 16479537,17981983, 15805522 19880604 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:16, 8 June 2011

  • Description: RNase, 3'-> 5' exoribonuclease

Gene name yhaM
Synonyms
Essential no
Product RNase YhaM
Function RNA degradation
MW, pI 35 kDa, 5.851
Gene length, protein length 942 bp, 314 aa
Immediate neighbours sbcE, yhaL
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YhaM context.gif
This image was kindly provided by SubtiList



Categories containing this gene/protein

Rnases

This gene is a member of the following regulons

LexA regulon

The gene

Basic information

  • Locus tag: BSU09930

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 3'-5' exoribonuclease
  • Protein family: OB DNA-binding domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: Cytoplasm (Homogeneous) PubMed

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

David Bechhofer, Mount Sinai School, New York, USA Homepage

Your additional remarks

References

Yulia Redko, Ciarán Condon
Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-III.
J Bacteriol: 2010, 192(1);356-9
[PubMed:19880604] [WorldCat.org] [DOI] (I p)

Ming Fang, Wencke-Maria Zeisberg, Ciaran Condon, Vasily Ogryzko, Antoine Danchin, Undine Mechold
Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis.
Nucleic Acids Res: 2009, 37(15);5114-25
[PubMed:19553197] [WorldCat.org] [DOI] (I p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [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)

Nora Au, Elke Kuester-Schoeck, Veena Mandava, Laura E Bothwell, Susan P Canny, Karen Chachu, Sierra A Colavito, Shakierah N Fuller, Eli S Groban, Laura A Hensley, Theresa C O'Brien, Amish Shah, Jessica T Tierney, Louise L Tomm, Thomas M O'Gara, Alexi I Goranov, Alan D Grossman, Charles M Lovett
Genetic composition of the Bacillus subtilis SOS system.
J Bacteriol: 2005, 187(22);7655-66
[PubMed:16267290] [WorldCat.org] [DOI] (P p)

Irina A Oussenko, Teppei Abe, Hiromi Ujiie, Akira Muto, David H Bechhofer
Participation of 3'-to-5' exoribonucleases in the turnover of Bacillus subtilis mRNA.
J Bacteriol: 2005, 187(8);2758-67
[PubMed:15805522] [WorldCat.org] [DOI] (P p)

Irina A Oussenko, Roberto Sanchez, David H Bechhofer
Bacillus subtilis YhaM, a member of a new family of 3'-to-5' exonucleases in gram-positive bacteria.
J Bacteriol: 2002, 184(22);6250-9
[PubMed:12399495] [WorldCat.org] [DOI] (P p)