Difference between revisions of "RnpA"

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* '''Description:''' protein component of [[RNase]] P, metal-dependent 5' end maturation of precursor [[tRNAs]] <br/><br/>
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* '''Description:''' protein component of [[RNase]] P, metal-dependent 5' end maturation of precursor [[tRNA]]s <br/><br/>
  
 
{| align="right" border="1" cellpadding="2"  
 
{| align="right" border="1" cellpadding="2"  
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|style="background:#ABCDEF;" align="center"| '''Product''' || protein component of [[RNase]] P (substrate specificity)  
 
|style="background:#ABCDEF;" align="center"| '''Product''' || protein component of [[RNase]] P (substrate specificity)  
 
|-
 
|-
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|style="background:#ABCDEF;" align="center"|'''Function''' || cleavage of precursor sequences <br/>from the 5' ends of pre-[[tRNAs]]
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|style="background:#ABCDEF;" align="center"|'''Function''' || cleavage of precursor sequences <br/>from the 5' ends of pre-[[tRNA]]s
 
|-
 
|-
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 13 kDa, 10.804   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 13 kDa, 10.804   
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
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* '''Catalyzed reaction/ biological activity:''' Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor (according to Swiss-Prot)  
+
* '''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)
 
* '''Protein family:''' rnpA family (according to Swiss-Prot)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
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* '''Interactions:''' [[RnpA]]-[[RpmH]],  RnpA-[[RnpB]]
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* '''[[Interactions]]:'''  
 +
** [[RnpA]]-[[RpmH]]
 +
** [[RnpA]]-[[RnpB]] {{PubMed|21622899}}
  
 
* '''Localization:'''
 
* '''Localization:'''
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* '''Structure:'''  
 
* '''Structure:'''  
 
** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1A6F 1AF6]  [http://www.ncbi.nlm.nih.gov/sites/entrez/9563955 PubMed]
 
** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1A6F 1AF6]  [http://www.ncbi.nlm.nih.gov/sites/entrez/9563955 PubMed]
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** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3OKB 3OKB] (complex of RnpA with the RNA RnpB and tRNA, from ''Thermotoga maritima'') {{PubMed|21076397}}
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** [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=3OKB 3OKB] (complex of RnpA with the RNA [[RnpB]] and [[tRNA]], from ''Thermotoga maritima'') {{PubMed|21076397}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P25814 P25814]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P25814 P25814]

Revision as of 08:29, 2 June 2011

  • Description: protein component of RNase P, metal-dependent 5' end maturation of precursor tRNAs

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




Categories containing this gene/protein

Rnases, translation, essential genes

This gene is a member of the following regulons

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:
  • 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

Your additional remarks

References

Reviews


Original Publications

Additional publications: PubMed

Yu-Chu Chang, Terrence G Oas
Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.
Biochemistry: 2010, 49(25);5086-96
[PubMed:20476778] [WorldCat.org] [DOI] (I p)

Kristin S Koutmou, Nathan H Zahler, Jeffrey C Kurz, Frank E Campbell, Michael E Harris, Carol A Fierke
Protein-precursor tRNA contact leads to sequence-specific recognition of 5' leaders by bacterial ribonuclease P.
J Mol Biol: 2010, 396(1);195-208
[PubMed:19932118] [WorldCat.org] [DOI] (I p)

John Hsieh, Carol A Fierke
Conformational change in the Bacillus subtilis RNase P holoenzyme--pre-tRNA complex enhances substrate affinity and limits cleavage rate.
RNA: 2009, 15(8);1565-77
[PubMed:19549719] [WorldCat.org] [DOI] (I p)

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)

Somashekarappa Niranjanakumari, Jeremy J Day-Storms, Mahiuddin Ahmed, John Hsieh, Nathan H Zahler, Ronald A Venters, Carol A Fierke
Probing the architecture of the B. subtilis RNase P holoenzyme active site by cross-linking and affinity cleavage.
RNA: 2007, 13(4);521-35
[PubMed:17299131] [WorldCat.org] [DOI] (P 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)

Christopher H Henkels, Terrence G Oas
Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein.
Biochemistry: 2005, 44(39);13014-26
[PubMed:16185070] [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)

C H Henkels, J C Kurz, C A Fierke, T G Oas
Linked folding and anion binding of the Bacillus subtilis ribonuclease P protein.
Biochemistry: 2001, 40(9);2777-89
[PubMed:11258888] [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)

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