RnjB
- Description: RNase J2
Gene name | rnjB |
Synonyms | ymfA |
Essential | no |
Product | RNase J2 |
Function | RNA processing and degradation |
Gene expression levels in SubtiExpress: rnjB | |
Interactions involving this protein in SubtInteract: RNase J2 | |
MW, pI | 56 kDa, 9.18 |
Gene length, protein length | 1545 bp, 515 aa |
Immediate neighbours | dapA, tepA |
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: BSU16780
Phenotypes of a mutant
Database entries
- BsubCyc: BSU16780
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: endoribonuclease, involved in processing of thrS mRNA
- Protein family: RNase J subfamily (according to Swiss-Prot)
- Paralogous protein(s): RnjA
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- associated to the RNA degradosome PubMed
- RnjA-RnjB PubMed
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- BsubCyc: BSU16780
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Regulation: constitutive expression PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP1113 (miniTn10 spc), available in Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Harald Putzer, IBPC Paris, France Homepage
Your additional remarks
References
Reviews
Original publications
Ailar Jamalli, Agnès Hébert, Léna Zig, Harald Putzer
Control of expression of the RNases J1 and J2 in Bacillus subtilis.
J Bacteriol: 2014, 196(2);318-24
[PubMed:24187087]
[WorldCat.org]
[DOI]
(I p)
Joseph A Newman, Lorraine Hewitt, Cecilia Rodrigues, Alexandra Solovyova, Colin R Harwood, Richard J Lewis
Unusual, dual endo- and exonuclease activity in the degradosome explained by crystal structure analysis of RNase J1.
Structure: 2011, 19(9);1241-51
[PubMed:21893285]
[WorldCat.org]
[DOI]
(I p)
Gintaras Deikus, David H Bechhofer
5' End-independent RNase J1 endonuclease cleavage of Bacillus subtilis model RNA.
J Biol Chem: 2011, 286(40);34932-40
[PubMed:21862575]
[WorldCat.org]
[DOI]
(I p)
Nathalie Mathy, Agnès Hébert, Peggy Mervelet, Lionel Bénard, Audrey Dorléans, Inés Li de la Sierra-Gallay, Philippe Noirot, Harald Putzer, Ciarán Condon
Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour.
Mol Microbiol: 2010, 75(2);489-98
[PubMed:20025672]
[WorldCat.org]
[DOI]
(I p)
Shiyi Yao, David H Bechhofer
Processing and stability of inducibly expressed rpsO mRNA derivatives in Bacillus subtilis.
J Bacteriol: 2009, 191(18);5680-9
[PubMed:19633085]
[WorldCat.org]
[DOI]
(I p)
Fabian M Commichau, Fabian M Rothe, Christina Herzberg, Eva Wagner, Daniel Hellwig, Martin Lehnik-Habrink, Elke Hammer, Uwe Völker, Jörg Stülke
Novel activities of glycolytic enzymes in Bacillus subtilis: interactions with essential proteins involved in mRNA processing.
Mol Cell Proteomics: 2009, 8(6);1350-60
[PubMed:19193632]
[WorldCat.org]
[DOI]
(I p)
Ulrike Mäder, Léna Zig, Julia Kretschmer, Georg Homuth, Harald Putzer
mRNA processing by RNases J1 and J2 affects Bacillus subtilis gene expression on a global scale.
Mol Microbiol: 2008, 70(1);183-96
[PubMed:18713320]
[WorldCat.org]
[DOI]
(I p)
Inés Li de la Sierra-Gallay, Léna Zig, Ailar Jamalli, Harald Putzer
Structural insights into the dual activity of RNase J.
Nat Struct Mol Biol: 2008, 15(2);206-12
[PubMed:18204464]
[WorldCat.org]
[DOI]
(I p)
Sergine Even, Olivier Pellegrini, Lena Zig, Valerie Labas, Joelle Vinh, Dominique Bréchemmier-Baey, Harald Putzer
Ribonucleases J1 and J2: two novel endoribonucleases in B.subtilis with functional homology to E.coli RNase E.
Nucleic Acids Res: 2005, 33(7);2141-52
[PubMed:15831787]
[WorldCat.org]
[DOI]
(I e)