Difference between revisions of "RnpA"

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=References=
 
=References=
  
<pubmed>11454206 9563955, </pubmed>
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<pubmed>10390342,17919279,17355991,11812129,16980484,11454206,,11454206 9563955, </pubmed>
 
# Hansen, A., Pfeiffer, T., Zuleeg, T., Limmer, S., Ciesiolka, J., Feltens, R. & Hartmann, R. K. (2001). Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzyme from ''Escherichia coli'' and ''Bacillus subtilis''. Mol Microbiol 41, 131-143. [http://www.ncbi.nlm.nih.gov/sites/entrez/11454206 PubMed]
 
# Hansen, A., Pfeiffer, T., Zuleeg, T., Limmer, S., Ciesiolka, J., Feltens, R. & Hartmann, R. K. (2001). Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzyme from ''Escherichia coli'' and ''Bacillus subtilis''. Mol Microbiol 41, 131-143. [http://www.ncbi.nlm.nih.gov/sites/entrez/11454206 PubMed]
 
# Stams T, Niranjanakumari S, Fierke CA, Christianson DW (1998) Ribonuclease P protein structure: evolutionary origins in the translational apparatus.''Science'' '''280:''' 752-755. [http://www.ncbi.nlm.nih.gov/sites/entrez/9563955 PubMed]
 
# Stams T, Niranjanakumari S, Fierke CA, Christianson DW (1998) Ribonuclease P protein structure: evolutionary origins in the translational apparatus.''Science'' '''280:''' 752-755. [http://www.ncbi.nlm.nih.gov/sites/entrez/9563955 PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]
 
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed]

Revision as of 09:50, 14 June 2009

  • Description: protein component of ribonuclease P

Gene name rnpA
Synonyms
Essential yes PubMed
Product protein component of RNase P (substrate specificity)
Function cleavage of precursor sequences
from the 5' ends of pre-tRNAs
MW, pI 13 kDa, 10.804
Gene length, protein length 348 bp, 116 aa
Immediate neighbours spoIIIJ, rpmH
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
ThdF jag spoIIIJ rnpA rpmH context.png
This image was kindly provided by SubtiList




The gene

Basic information

  • Locus tag: BSU41050

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor (according to Swiss-Prot)
  • Protein family: rnpA family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • KEGG entry: [2]

Additional information

Expression and regulation

  • Operon:
  • 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

Roland Hartmann, Marburg University, Germany homepage

Your additional remarks

References

Markus Gösringer, Roland K Hartmann
Function of heterologous and truncated RNase P proteins in Bacillus subtilis.
Mol Microbiol: 2007, 66(3);801-13
[PubMed:17919279] [WorldCat.org] [DOI] (P p)

Barbara Wegscheid, Roland K Hartmann
In vivo and in vitro investigation of bacterial type B RNase P interaction with tRNA 3'-CCA.
Nucleic Acids Res: 2007, 35(6);2060-73
[PubMed:17355991] [WorldCat.org] [DOI] (I p)

Markus Gössringer, Rosel Kretschmer-Kazemi Far, Roland K Hartmann
Analysis of RNase P protein (rnpA) expression in Bacillus subtilis utilizing strains with suppressible rnpA expression.
J Bacteriol: 2006, 188(19);6816-23
[PubMed:16980484] [WorldCat.org] [DOI] (P p)

Christoph Rox, Ralph Feltens, Thomas Pfeiffer, Roland K Hartmann
Potential contact sites between the protein and RNA subunit in the Bacillus subtilis RNase P holoenzyme.
J Mol Biol: 2002, 315(4);551-60
[PubMed:11812129] [WorldCat.org] [DOI] (P p)

A Hansen, T Pfeiffer, T Zuleeg, S Limmer, J Ciesiolka, R Feltens, R K Hartmann
Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis.
Mol Microbiol: 2001, 41(1);131-43
[PubMed:11454206] [WorldCat.org] [DOI] (P p)

J M Warnecke, R Held, S Busch, R K Hartmann
Role of metal ions in the hydrolysis reaction catalyzed by RNase P RNA from Bacillus subtilis.
J Mol Biol: 1999, 290(2);433-45
[PubMed:10390342] [WorldCat.org] [DOI] (P p)

T Stams, S Niranjanakumari, C A Fierke, D W Christianson
Ribonuclease P protein structure: evolutionary origins in the translational apparatus.
Science: 1998, 280(5364);752-5
[PubMed:9563955] [WorldCat.org] [DOI] (P p)

  1. Hansen, A., Pfeiffer, T., Zuleeg, T., Limmer, S., Ciesiolka, J., Feltens, R. & Hartmann, R. K. (2001). Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzyme from Escherichia coli and Bacillus subtilis. Mol Microbiol 41, 131-143. PubMed
  2. Stams T, Niranjanakumari S, Fierke CA, Christianson DW (1998) Ribonuclease P protein structure: evolutionary origins in the translational apparatus.Science 280: 752-755. PubMed
  3. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed