Difference between revisions of "RnpA"
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* '''[[Interactions]]:''' | * '''[[Interactions]]:''' | ||
+ | ** forms dimers {{PubMed|21764917}} | ||
** [[RnpA]]-[[RpmH]] | ** [[RnpA]]-[[RpmH]] | ||
** [[RnpA]]-[[RnpB]] {{PubMed|21622899}} | ** [[RnpA]]-[[RnpB]] {{PubMed|21622899}} | ||
+ | ** [[RnpA]]-[[CshA]] {{PubMed|21764917}} | ||
* '''Localization:''' | * '''Localization:''' |
Revision as of 17:35, 19 July 2011
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 This image was kindly provided by SubtiList
|
Contents
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:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization:
Database entries
- Structure:
- UniProt: P25814
- KEGG entry: [2]
- E.C. number: 3.1.26.5
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
- Carol Fierke, University of Michigan, Ann Arbor, USA homepage
- Roland Hartmann, Marburg University, Germany homepage
Your additional remarks
References
Reviews
Roland K Hartmann, Markus Gössringer, Bettina Späth, Susan Fischer, Anita Marchfelder
The making of tRNAs and more - RNase P and tRNase Z.
Prog Mol Biol Transl Sci: 2009, 85;319-68
[PubMed:19215776]
[WorldCat.org]
[DOI]
(P p)
J Kristin Smith, John Hsieh, Carol A Fierke
Importance of RNA-protein interactions in bacterial ribonuclease P structure and catalysis.
Biopolymers: 2007, 87(5-6);329-38
[PubMed:17868095]
[WorldCat.org]
[DOI]
(P p)
Alexei V Kazantsev, Norman R Pace
Bacterial RNase P: a new view of an ancient enzyme.
Nat Rev Microbiol: 2006, 4(10);729-40
[PubMed:16980936]
[WorldCat.org]
[DOI]
(I p)
Donald Evans, Steven M Marquez, Norman R Pace
RNase P: interface of the RNA and protein worlds.
Trends Biochem Sci: 2006, 31(6);333-41
[PubMed:16679018]
[WorldCat.org]
[DOI]
(P p)
Alfredo Torres-Larios, Kerren K Swinger, Tao Pan, Alfonso Mondragón
Structure of ribonuclease P--a universal ribozyme.
Curr Opin Struct Biol: 2006, 16(3);327-35
[PubMed:16650980]
[WorldCat.org]
[DOI]
(P p)
John Hsieh, Andy J Andrews, Carol A Fierke
Roles of protein subunits in RNA-protein complexes: lessons from ribonuclease P.
Biopolymers: 2004, 73(1);79-89
[PubMed:14691942]
[WorldCat.org]
[DOI]
(P p)
Enno Hartmann, Roland K Hartmann
The enigma of ribonuclease P evolution.
Trends Genet: 2003, 19(10);561-9
[PubMed:14550630]
[WorldCat.org]
[DOI]
(P p)
L A Kirsebom, A Vioque
RNase P from bacteria. Substrate recognition and function of the protein subunit.
Mol Biol Rep: 1995, 22(2-3);99-109
[PubMed:8901495]
[WorldCat.org]
[DOI]
(P p)
Original Publications
Additional publications: PubMed