Difference between revisions of "Rnz"

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(Original Publications)
 
(3 intermediate revisions by the same user not shown)
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 921 bp, 307 aa  
 
|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 921 bp, 307 aa  
 
|-
 
|-
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yqjL]]'', ''[[zwf]]''
+
|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[rpmGC]]'', ''[[zwf]]''
 
|-
 
|-
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23840 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23840 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23840 DNA_with_flanks]
 
|style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU23840 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU23840 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU23840 DNA_with_flanks]
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=== Additional information===
 
=== Additional information===
 
 
 
  
 
=The protein=
 
=The protein=
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=== Basic information/ Evolution ===
 
=== Basic information/ Evolution ===
  
* '''Catalyzed reaction/ biological activity:''' Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs (according to Swiss-Prot)  
+
* '''Catalyzed reaction/ biological activity:'''  
 +
** Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs (according to Swiss-Prot)  
 +
** 3' end maturation of tmRNA {{PubMed|25402410}}
  
 
* '''Protein family:''' [[RNase]] Z family (according to Swiss-Prot)
 
* '''Protein family:''' [[RNase]] Z family (according to Swiss-Prot)
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=References=
 
=References=
 
==Reviews==
 
==Reviews==
<pubmed> 19215776 17599240 </pubmed>
+
<pubmed> 19215776 17599240 25878039</pubmed>
  
 
==Original Publications==
 
==Original Publications==
<pubmed>17005971 12941704 15654328 16518398 22940585</pubmed>
+
<pubmed>17005971 12941704 15654328 16518398 22940585 25402410  24022488</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Latest revision as of 15:09, 26 April 2015

Gene name rnz
Synonyms yqjK
Essential yes PubMed
Product endoribonuclease Z
Function processing of CCA-less tRNA precursors
Gene expression levels in SubtiExpress: rnz
MW, pI 33 kDa, 5.805
Gene length, protein length 921 bp, 307 aa
Immediate neighbours rpmGC, zwf
Sequences Protein DNA DNA_with_flanks
Genetic context
YqjK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Rnz expression.png















Categories containing this gene/protein

Rnases, translation, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU23840

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs (according to Swiss-Prot)
    • 3' end maturation of tmRNA PubMed
  • Protein family: RNase Z family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Operon: rnz (according to DBTBS)
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 55 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 278 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 379 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 311 PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Ciaran Condon, IBPC, Paris, France Homepage

Your additional remarks

References

Reviews

Murray P Deutscher
How bacterial cells keep ribonucleases under control.
FEMS Microbiol Rev: 2015, 39(3);350-61
[PubMed:25878039] [WorldCat.org] [DOI] (I p)

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)

B Späth, G Canino, A Marchfelder
tRNase Z: the end is not in sight.
Cell Mol Life Sci: 2007, 64(18);2404-12
[PubMed:17599240] [WorldCat.org] [DOI] (P p)


Original Publications

Laetitia Gilet, Jeanne M DiChiara, Sabine Figaro, David H Bechhofer, Ciarán Condon
Small stable RNA maturation and turnover in Bacillus subtilis.
Mol Microbiol: 2015, 95(2);270-82
[PubMed:25402410] [WorldCat.org] [DOI] (I p)

Tanmay Dutta, Arun Malhotra, Murray P Deutscher
How a CCA sequence protects mature tRNAs and tRNA precursors from action of the processing enzyme RNase BN/RNase Z.
J Biol Chem: 2013, 288(42);30636-30644
[PubMed:24022488] [WorldCat.org] [DOI] (I p)

Olivier Pellegrini, Inés Li de la Sierra-Gallay, Jérémie Piton, Laetitia Gilet, Ciarán Condon
Activation of tRNA maturation by downstream uracil residues in B. subtilis.
Structure: 2012, 20(10);1769-77
[PubMed:22940585] [WorldCat.org] [DOI] (I 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)

Inés Li de la Sierra-Gallay, Nathalie Mathy, Olivier Pellegrini, Ciarán Condon
Structure of the ubiquitous 3' processing enzyme RNase Z bound to transfer RNA.
Nat Struct Mol Biol: 2006, 13(4);376-7
[PubMed:16518398] [WorldCat.org] [DOI] (P p)

Inés Li de la Sierra-Gallay, Olivier Pellegrini, Ciarán Condon
Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z.
Nature: 2005, 433(7026);657-61
[PubMed:15654328] [WorldCat.org] [DOI] (I p)

Olivier Pellegrini, Jamel Nezzar, Anita Marchfelder, Harald Putzer, Ciarán Condon
Endonucleolytic processing of CCA-less tRNA precursors by RNase Z in Bacillus subtilis.
EMBO J: 2003, 22(17);4534-43
[PubMed:12941704] [WorldCat.org] [DOI] (P p)