Difference between revisions of "RnhC"

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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[zapA]]'', ''[[pheT]]''
 
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[zapA]]'', ''[[pheT]]''
 
|-
 
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28620 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28620 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28620 Advanced_DNA]
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|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU28620 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU28620 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU28620 DNA_with_flanks]
 
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|colspan="2" | '''Genetic context''' <br/> [[Image:rnhC_context.gif]]
 
|colspan="2" | '''Genetic context''' <br/> [[Image:rnhC_context.gif]]

Revision as of 10:57, 14 May 2013

  • Description: RNase HIII, endoribonuclease

Gene name rnhC
Synonyms ysgB
Essential no
Product Mg2+-dependent RNase HIII
Function endonucleolytic cleavage of RNA
in RNA-DNA hybrid molecules
Gene expression levels in SubtiExpress: rnhC
MW, pI 33 kDa, 10.07
Gene length, protein length 939 bp, 313 aa
Immediate neighbours zapA, pheT
Sequences Protein DNA DNA_with_flanks
Genetic context
RnhC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RnhC expression.png


























Categories containing this gene/protein

Rnases

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU28620

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endonucleolytic cleavage to 5'-phosphomonoester (according to Swiss-Prot)
  • Protein family: RnhC subfamily (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: 2D0B (complex with Mg2+, Geobacillus stearothermophilus , 47% identity), 2D0A (Geobacillus stearothermophilus, 47% identity)
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • 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

Takashi Tadokoro, Shigenori Kanaya
Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.
FEBS J: 2009, 276(6);1482-93
[PubMed:19228197] [WorldCat.org] [DOI] (I p)

Original publications

Additional publications: PubMed

Sanae Fukushima, Mitsuhiro Itaya, Hiroaki Kato, Naotake Ogasawara, Hirofumi Yoshikawa
Reassessment of the in vivo functions of DNA polymerase I and RNase H in bacterial cell growth.
J Bacteriol: 2007, 189(23);8575-83
[PubMed:17905985] [WorldCat.org] [DOI] (I p)

M Itaya, A Omori, S Kanaya, R J Crouch, T Tanaka, K Kondo
Isolation of RNase H genes that are essential for growth of Bacillus subtilis 168.
J Bacteriol: 1999, 181(7);2118-23
[PubMed:10094689] [WorldCat.org] [DOI] (P p)

N Ohtani, M Haruki, M Morikawa, R J Crouch, M Itaya, S Kanaya
Identification of the genes encoding Mn2+-dependent RNase HII and Mg2+-dependent RNase HIII from Bacillus subtilis: classification of RNases H into three families.
Biochemistry: 1999, 38(2);605-18
[PubMed:9888800] [WorldCat.org] [DOI] (P p)

A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504] [WorldCat.org] [DOI] (P p)