Difference between revisions of "RnjA"

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(Expression and regulation)
(Reviews)
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed>20458164 21334965 21893280 23403287,21957024 22568516 24064983 </pubmed>
+
<pubmed>20458164 21334965 21893280 23403287,21957024 22568516 24064983 25292357</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 24187087</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 24187087</pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:28, 8 March 2015

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:
rnjA
MW, pI 61 kDa, 5.902
Gene length, protein length 1665 bp, 555 aa
Immediate neighbours adeC, rpoY
Sequences Protein DNA DNA_with_flanks
Genetic context
YkqC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
RnjA expression.png















Categories containing this gene/protein

Rnases, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU14530

Phenotypes of a mutant

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:

Database entries

  • 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

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • translation of YkzG and RnjA is coupled, and this coupling is required for efficient expression of RNase J1 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 2868 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 4928 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2768 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4125 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 5056 PubMed

Biological materials

  • Mutant:
    • GP41 (rnjA under control of p(xyl)), available in Jörg Stülke's 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
  • GFP fusion:
  • two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), 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

Monica P Hui, Patricia L Foley, Joel G Belasco
Messenger RNA degradation in bacterial cells.
Annu Rev Genet: 2014, 48;537-59
[PubMed:25292357] [WorldCat.org] [DOI] (I p)

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

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)

Sabine Figaro, Sylvain Durand, Laetitia Gilet, Nadège Cayet, Martin Sachse, Ciarán Condon
Bacillus subtilis mutants with knockouts of the genes encoding ribonucleases RNase Y and RNase J1 are viable, with major defects in cell morphology, sporulation, and competence.
J Bacteriol: 2013, 195(10);2340-8
[PubMed:23504012] [WorldCat.org] [DOI] (I p)

Sylvain Durand, Laetitia Gilet, Philippe Bessières, Pierre Nicolas, Ciarán Condon
Three essential ribonucleases-RNase Y, J1, and III-control the abundance of a majority of Bacillus subtilis mRNAs.
PLoS Genet: 2012, 8(3);e1002520
[PubMed:22412379] [WorldCat.org] [DOI] (I p)

Joseph A Newman, Lorraine Hewitt, Cecilia Rodrigues, Alexandra S Solovyova, Colin R Harwood, Richard J Lewis
Dissection of the network of interactions that links RNA processing with glycolysis in the Bacillus subtilis degradosome.
J Mol Biol: 2012, 416(1);121-36
[PubMed:22198292] [WorldCat.org] [DOI] (I p)

Jamie Richards, Quansheng Liu, Olivier Pellegrini, Helena Celesnik, Shiyi Yao, David H Bechhofer, Ciarán Condon, Joel G Belasco
An RNA pyrophosphohydrolase triggers 5'-exonucleolytic degradation of mRNA in Bacillus subtilis.
Mol Cell: 2011, 43(6);940-9
[PubMed:21925382] [WorldCat.org] [DOI] (I p)

Shiyi Yao, Jamie Richards, Joel G Belasco, David H Bechhofer
Decay of a model mRNA in Bacillus subtilis by a combination of RNase J1 5' exonuclease and RNase Y endonuclease activities.
J Bacteriol: 2011, 193(22);6384-6
[PubMed:21908660] [WorldCat.org] [DOI] (I p)

Audrey Dorléans, Inés Li de la Sierra-Gallay, Jérémie Piton, Léna Zig, Laetitia Gilet, Harald Putzer, Ciarán Condon
Molecular basis for the recognition and cleavage of RNA by the bifunctional 5'-3' exo/endoribonuclease RNase J.
Structure: 2011, 19(9);1252-61
[PubMed:21893286] [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)

Martin Lehnik-Habrink, Joseph Newman, Fabian M Rothe, Alexandra S Solovyova, Cecilia Rodrigues, Christina Herzberg, Fabian M Commichau, Richard J Lewis, Jörg Stülke
RNase Y in Bacillus subtilis: a Natively disordered protein that is the functional equivalent of RNase E from Escherichia coli.
J Bacteriol: 2011, 193(19);5431-41
[PubMed:21803996] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Henrike Pförtner, Leonie Rempeters, Nico Pietack, Christina Herzberg, Jörg Stülke
The RNA degradosome in Bacillus subtilis: identification of CshA as the major RNA helicase in the multiprotein complex.
Mol Microbiol: 2010, 77(4);958-71
[PubMed:20572937] [WorldCat.org] [DOI] (I p)

Shiyi Yao, David H Bechhofer
Initiation of decay of Bacillus subtilis rpsO mRNA by endoribonuclease RNase Y.
J Bacteriol: 2010, 192(13);3279-86
[PubMed:20418391] [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)

Yulia Redko, Ciarán Condon
Maturation of 23S rRNA in Bacillus subtilis in the absence of Mini-III.
J Bacteriol: 2010, 192(1);356-9
[PubMed:19880604] [WorldCat.org] [DOI] (I p)

Shiyi Yao, Josh S Sharp, David H Bechhofer
Bacillus subtilis RNase J1 endonuclease and 5' exonuclease activities in the turnover of DeltaermC mRNA.
RNA: 2009, 15(12);2331-9
[PubMed:19850915] [WorldCat.org] [DOI] (I p)

Gintaras Deikus, David H Bechhofer
Bacillus subtilis trp Leader RNA: RNase J1 endonuclease cleavage specificity and PNPase processing.
J Biol Chem: 2009, 284(39);26394-401
[PubMed:19638340] [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)

Ming Fang, Wencke-Maria Zeisberg, Ciaran Condon, Vasily Ogryzko, Antoine Danchin, Undine Mechold
Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis.
Nucleic Acids Res: 2009, 37(15);5114-25
[PubMed:19553197] [WorldCat.org] [DOI] (I p)

Roula Daou-Chabo, Ciarán Condon
RNase J1 endonuclease activity as a probe of RNA secondary structure.
RNA: 2009, 15(7);1417-25
[PubMed:19458035] [WorldCat.org] [DOI] (I p)

Roula Daou-Chabo, Nathalie Mathy, Lionel Bénard, Ciarán Condon
Ribosomes initiating translation of the hbs mRNA protect it from 5'-to-3' exoribonucleolytic degradation by RNase J1.
Mol Microbiol: 2009, 71(6);1538-50
[PubMed:19210617] [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)

Gintaras Deikus, Ciarán Condon, David H Bechhofer
Role of Bacillus subtilis RNase J1 endonuclease and 5'-exonuclease activities in trp leader RNA turnover.
J Biol Chem: 2008, 283(25);17158-67
[PubMed:18445592] [WorldCat.org] [DOI] (P 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)

Jennifer A Collins, Irnov Irnov, Stephanie Baker, Wade C Winkler
Mechanism of mRNA destabilization by the glmS ribozyme.
Genes Dev: 2007, 21(24);3356-68
[PubMed:18079181] [WorldCat.org] [DOI] (P p)

Ulf Gerth, Holger Kock, Ilja Kusters, Stephan Michalik, Robert L Switzer, Michael Hecker
Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.
J Bacteriol: 2008, 190(1);321-31
[PubMed:17981983] [WorldCat.org] [DOI] (I p)

Shiyi Yao, Joshua B Blaustein, David H Bechhofer
Processing of Bacillus subtilis small cytoplasmic RNA: evidence for an additional endonuclease cleavage site.
Nucleic Acids Res: 2007, 35(13);4464-73
[PubMed:17576666] [WorldCat.org] [DOI] (I p)

Nathalie Mathy, Lionel Bénard, Olivier Pellegrini, Roula Daou, Tingyi Wen, Ciarán Condon
5'-to-3' exoribonuclease activity in bacteria: role of RNase J1 in rRNA maturation and 5' stability of mRNA.
Cell: 2007, 129(4);681-92
[PubMed:17512403] [WorldCat.org] [DOI] (P p)

Robert A Britton, Tingyi Wen, Laura Schaefer, Olivier Pellegrini, William C Uicker, Nathalie Mathy, Crystal Tobin, Roula Daou, Jacek Szyk, Ciarán Condon
Maturation of the 5' end of Bacillus subtilis 16S rRNA by the essential ribonuclease YkqC/RNase J1.
Mol Microbiol: 2007, 63(1);127-38
[PubMed:17229210] [WorldCat.org] [DOI] (P p)

Alison Hunt, Joy P Rawlins, Helena B Thomaides, Jeff Errington
Functional analysis of 11 putative essential genes in Bacillus subtilis.
Microbiology (Reading): 2006, 152(Pt 10);2895-2907
[PubMed:17005971] [WorldCat.org] [DOI] (P 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)