Difference between revisions of "Rnr"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU33610&redirect=T BSU33610]
  
 
* '''DBTBS entry:''' no entry
 
* '''DBTBS entry:''' no entry
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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU33610&redirect=T BSU33610]
  
 
* '''Structure:'''
 
* '''Structure:'''

Revision as of 14:45, 2 April 2014

  • Description: RNase R, required for protection against paraquat stress

Gene name rnr
Synonyms yvaJ
Essential no
Product exoribonuclease RNase R (EC 3.1.-.-)
Function nonspecific degradation of rRNA
Gene expression levels in SubtiExpress: rnr
MW, pI 88 kDa, 5.703
Gene length, protein length 2337 bp, 779 aa
Immediate neighbours smpB, yvaK
Sequences Protein DNA DNA_with_flanks
Genetic context
Rnr context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Rnr expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, Rnases, resistance against oxidative and electrophile stress

This gene is a member of the following regulons

SigB regulon

The gene

Basic information

  • Locus tag: BSU33610

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 3'-5'-exoribonuclease
  • Protein family: ribonuclease II (RNB) family (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: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Regulatory mechanism:
  • Additional information:

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

Andrés Cruz Hernández, Emmanuel Sánchez Millan, Sergio de Jesús Romero Gómez, José Antonio Cervantes Chávez, Rocio Garcia Martínez, Xóchitl Pastrana Martínez, Jackeline Lizzeta Arvizu Gómez, George H Jones, Juan Campos Guillén
Exposure of Bacillus subtilis to mercury induces accumulation of shorter tRNA Cys species.
Metallomics: 2013, 5(4);398-403
[PubMed:23529473] [WorldCat.org] [DOI] (I p)

Alexander Reder, Dirk Höper, Ulf Gerth, Michael Hecker
Contributions of individual σB-dependent general stress genes to oxidative stress resistance of Bacillus subtilis.
J Bacteriol: 2012, 194(14);3601-10
[PubMed:22582280] [WorldCat.org] [DOI] (I p)

Juan Campos-Guillén, Jackeline Lizzeta Arvizu-Gómez, George H Jones, Gabriela Olmedo-Alvarez
Characterization of tRNA(Cys) processing in a conditional Bacillus subtilis CCase mutant reveals the participation of RNase R in its quality control.
Microbiology (Reading): 2010, 156(Pt 7);2102-2111
[PubMed:20360175] [WorldCat.org] [DOI] (I p)

Ji-Hyun Shin, Chester W Price
The SsrA-SmpB ribosome rescue system is important for growth of Bacillus subtilis at low and high temperatures.
J Bacteriol: 2007, 189(10);3729-37
[PubMed:17369301] [WorldCat.org] [DOI] (P p)

Dirk Höper, Uwe Völker, Michael Hecker
Comprehensive characterization of the contribution of individual SigB-dependent general stress genes to stress resistance of Bacillus subtilis.
J Bacteriol: 2005, 187(8);2810-26
[PubMed:15805528] [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)