Difference between revisions of "RnjA"
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− | <pubmed>20458164 21334965 21893280 23403287,21957024 22568516</pubmed> | + | <pubmed>20458164 21334965 21893280 23403287,21957024 22568516 24064983 </pubmed> |
==Original publications== | ==Original publications== | ||
<pubmed>18079181, 19553197, 17981983, 19458035, 15831787, 18204464, 18713320, 19193632, 17005971, 18445592, 17512403, 17229210, 17576666, 19210617 19633085 19638340 19850915 19880604 20025672 20418391 20572937 ,21803996 21862575 21925382 22198292 22412379 23504012 21893285,21893286,21908660</pubmed> | <pubmed>18079181, 19553197, 17981983, 19458035, 15831787, 18204464, 18713320, 19193632, 17005971, 18445592, 17512403, 17229210, 17576666, 19210617 19633085 19638340 19850915 19880604 20025672 20418391 20572937 ,21803996 21862575 21925382 22198292 22412379 23504012 21893285,21893286,21908660</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 17:02, 13 November 2013
- Description: RNase J1
Gene name | rnjA |
Synonyms | ykqC |
Essential | yes PubMed |
Product | RNase J1 |
Function | RNA processing |
Gene expression levels in SubtiExpress: rnjA | |
Interactions involving this protein in SubtInteract: RNase J1 | |
Metabolic function and regulation of this protein in SubtiPathways: Ile, Leu, Val, Coenzyme A | |
MW, pI | 61 kDa, 5.902 |
Gene length, protein length | 1665 bp, 555 aa |
Immediate neighbours | adeC, ykzG |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14530
Phenotypes of a mutant
- essential PubMed
- a study from the lab of Ciaran Condon reports that rnjA is non-essential and that the mutant is strongly impaired in sporulation, genetic competence and many other phenotypes PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: endonuclease and 5'-3' exonuclease
- Protein family: RNase J subfamily (according to Swiss-Prot)
- Paralogous protein(s): RnjB
RNAs affected by rnjA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: Q45493
- KEGG entry: [2]
- E.C. number:
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
- required for thrS RNA processing, involved in maturation of the 5’-end of the16S rRNA
Expression and regulation
- Operon:
- Regulation:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant: GP41 (rnjA under control of p(xyl)), available in Stülke lab; SSB342 (rnjA under pspac), cat, available in Harald Putzer lab
- Expression vector:
- for chromosomal expression of RNase J1-Strep (spc): GP1034, available in Jörg Stülke's lab
- for chromosomal expression of RNase J1-Strep (cat): GP1042, available in Jörg Stülke's lab
- lacZ fusion: pGP418 (in pAC7), available in Jörg Stülke's lab
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- FLAG-tag construct:
- GP1020 (spc, based on pGP1331), available in Jörg Stülke's lab
- GP1075 (aphA3), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Harald Putzer, IBPC Paris, France Homepage
David Bechhofer, Mount Sinai School, New York, USA Homepage
Ciaran Condon, IBPC, Paris, France Homepage
Your additional remarks
References
Reviews
Soumaya Laalami, Léna Zig, Harald Putzer
Initiation of mRNA decay in bacteria.
Cell Mol Life Sci: 2014, 71(10);1799-828
[PubMed:24064983]
[WorldCat.org]
[DOI]
(I p)
Zbigniew Dominski, Agamemnon J Carpousis, Béatrice Clouet-d'Orval
Emergence of the β-CASP ribonucleases: highly conserved and ubiquitous metallo-enzymes involved in messenger RNA maturation and degradation.
Biochim Biophys Acta: 2013, 1829(6-7);532-51
[PubMed:23403287]
[WorldCat.org]
[DOI]
(P p)
Martin Lehnik-Habrink, Richard J Lewis, Ulrike Mäder, Jörg Stülke
RNA degradation in Bacillus subtilis: an interplay of essential endo- and exoribonucleases.
Mol Microbiol: 2012, 84(6);1005-17
[PubMed:22568516]
[WorldCat.org]
[DOI]
(I p)
David H Bechhofer
Bacillus subtilis mRNA decay: new parts in the toolkit.
Wiley Interdiscip Rev RNA: 2011, 2(3);387-94
[PubMed:21957024]
[WorldCat.org]
[DOI]
(I p)
Jamie Richards, Joel G Belasco
Ribonuclease J: how to lead a double life.
Structure: 2011, 19(9);1201-3
[PubMed:21893280]
[WorldCat.org]
[DOI]
(I p)
Ciarán Condon, David H Bechhofer
Regulated RNA stability in the Gram positives.
Curr Opin Microbiol: 2011, 14(2);148-54
[PubMed:21334965]
[WorldCat.org]
[DOI]
(I p)
Ciarán Condon
What is the role of RNase J in mRNA turnover?
RNA Biol: 2010, 7(3);316-21
[PubMed:20458164]
[WorldCat.org]
[DOI]
(I p)
Original publications