Difference between revisions of "YhaM"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[sbcE]]'', ''[[yhaL]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[sbcE]]'', ''[[yhaL]]''
 
|-
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU09930 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU09930 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU09930 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU09930 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU09930 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU09930 DNA_with_flanks]
 
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|-
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yhaM_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:yhaM_context.gif]]

Revision as of 09:49, 14 May 2013

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

Gene name yhaM
Synonyms
Essential no
Product RNase YhaM
Function RNA degradation
Gene expression levels in SubtiExpress: yhaM
MW, pI 35 kDa, 5.851
Gene length, protein length 942 bp, 314 aa
Immediate neighbours sbcE, yhaL
Sequences Protein DNA DNA_with_flanks
Genetic context
YhaM context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YhaM expression.png
























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:

Database entries

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

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Sigma factor:
  • 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)

Rita A Eckart, Sabine Brantl, Andreas Licht
Search for additional targets of the transcriptional regulator CcpN from Bacillus subtilis.
FEMS Microbiol Lett: 2009, 299(2);223-31
[PubMed:19732150] [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)