Difference between revisions of "MutTA"

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* '''Catalyzed reaction/ biological activity:'''  
 
* '''Catalyzed reaction/ biological activity:'''  
 
** removal of pyrophosphate from the 5' end of mRNAs to make the RNA accessible for degradation by [[RNases]] {{PubMed|21925382}}  
 
** removal of pyrophosphate from the 5' end of mRNAs to make the RNA accessible for degradation by [[RNases]] {{PubMed|21925382}}  
 +
** RppH requires at least two unpaired nucleotides at the 5' end of its RNA substrates and prefers three or more. The second of these 5'-terminal nucleotides must be G, whereas a less strict preference for a purine is evident at the third position, and A is slightly favored over G at the first position {{PubMed|23610425,23610407}}
  
 
* '''Protein family:''' [[Nudix hydrolase]] family (according to Swiss-Prot)
 
* '''Protein family:''' [[Nudix hydrolase]] family (according to Swiss-Prot)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:'''
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* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=4JZV 4JZV] {{PubMed|23610407}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O35013 O35013]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/O35013 O35013]
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ytkD_3134983_3135459_-1 mutTA] {{PubMed|22383849}}
 
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=ytkD_3134983_3135459_-1 mutTA] {{PubMed|22383849}}
  
* '''Sigma factor:''' [[SigA]] {{PubMed|14761999}}, [[SigF]] {{PubMed|14761999}}
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* '''[[Sigma factor]]:''' [[SigA]] {{PubMed|14761999}}, [[SigF]] {{PubMed|14761999}}
  
 
* '''Regulation:'''  
 
* '''Regulation:'''  
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=References=
 
=References=
 
== Reviews ==
 
== Reviews ==
<big>''Lehnik-Habrink M, Lewis RJ, Mäder U, Stülke J''  </big>
+
<pubmed> 22568516</pubmed>
<big>'''RNA degradation in ''Bacillus subtilis'': an interplay of</big>
 
<big>'''essential endo- and exoribonucleases.''' </big>
 
<big>Mol Microbiol.: 2012, 84(6) 1005-1017. </big>
 
[http://www.ncbi.nlm.nih.gov/pubmed/22568516 PubMed:22568516]
 
 
== Original publications ==
 
== Original publications ==
<pubmed>16513759,16497325, 14761999, 19011023 9387221 15576788 21925382 </pubmed>
+
<pubmed>16513759,16497325, 14761999, 19011023 9387221 15576788 21925382 23610425 23610407 </pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 07:42, 25 April 2013

  • Description: error prevention oxidized guanine system, confers protection against oxidative stress to vegetative cells, moreover the protein has RNA pyrophosphohydrolase activity

Gene name mutTA
Synonyms ytkD, rppH
Essential no
Product 8-oxo-dGTPase (antimutator), RNA pyrophosphohydrolase
Function DNA repair, RNA degradation
Gene expression levels in SubtiExpress: mutTA
MW, pI 18 kDa, 5.952
Gene length, protein length 474 bp, 158 aa
Immediate neighbours ytlD, ytkC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YtkD context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MutTA expression.png















Categories containing this gene/protein

DNA repair/ recombination, sporulation proteins, RNases

This gene is a member of the following regulons

SigF regulon

The gene

Basic information

  • Locus tag: BSU30630

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
    • removal of pyrophosphate from the 5' end of mRNAs to make the RNA accessible for degradation by RNases PubMed
    • RppH requires at least two unpaired nucleotides at the 5' end of its RNA substrates and prefers three or more. The second of these 5'-terminal nucleotides must be G, whereas a less strict preference for a purine is evident at the third position, and A is slightly favored over G at the first position PubMed
  • 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

  • Regulation:
    • expressed during logarithmic growth (SigA) and early during sporulation in the forespore (SigF) PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

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)

Original publications

Ping-kun Hsieh, Jamie Richards, Quansheng Liu, Joel G Belasco
Specificity of RppH-dependent RNA degradation in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2013, 110(22);8864-9
[PubMed:23610425] [WorldCat.org] [DOI] (I p)

Jérémie Piton, Valéry Larue, Yann Thillier, Audrey Dorléans, Olivier Pellegrini, Inés Li de la Sierra-Gallay, Jean-Jacques Vasseur, Françoise Debart, Carine Tisné, Ciarán Condon
Bacillus subtilis RNA deprotection enzyme RppH recognizes guanosine in the second position of its substrates.
Proc Natl Acad Sci U S A: 2013, 110(22);8858-63
[PubMed:23610407] [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)

Luz E Vidales, Lluvia C Cárdenas, Eduardo Robleto, Ronald E Yasbin, Mario Pedraza-Reyes
Defects in the error prevention oxidized guanine system potentiate stationary-phase mutagenesis in Bacillus subtilis.
J Bacteriol: 2009, 191(2);506-13
[PubMed:19011023] [WorldCat.org] [DOI] (I p)

Francisco X Castellanos-Juárez, Carlos Alvarez-Alvarez, Ronald E Yasbin, Barbara Setlow, Peter Setlow, Mario Pedraza-Reyes
YtkD and MutT protect vegetative cells but not spores of Bacillus subtilis from oxidative stress.
J Bacteriol: 2006, 188(6);2285-9
[PubMed:16513759] [WorldCat.org] [DOI] (P p)

Stephanie T Wang, Barbara Setlow, Erin M Conlon, Jessica L Lyon, Daisuke Imamura, Tsutomu Sato, Peter Setlow, Richard Losick, Patrick Eichenberger
The forespore line of gene expression in Bacillus subtilis.
J Mol Biol: 2006, 358(1);16-37
[PubMed:16497325] [WorldCat.org] [DOI] (P p)

Wenlian Xu, Candice R Jones, Christopher A Dunn, Maurice J Bessman
Gene ytkD of Bacillus subtilis encodes an atypical nucleoside triphosphatase member of the Nudix hydrolase superfamily.
J Bacteriol: 2004, 186(24);8380-4
[PubMed:15576788] [WorldCat.org] [DOI] (P p)

Martha I Ramírez, Francisco X Castellanos-Juárez, Ronald E Yasbin, Mario Pedraza-Reyes
The ytkD (mutTA) gene of Bacillus subtilis encodes a functional antimutator 8-Oxo-(dGTP/GTP)ase and is under dual control of sigma A and sigma F RNA polymerases.
J Bacteriol: 2004, 186(4);1050-9
[PubMed:14761999] [WorldCat.org] [DOI] (P p)

Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221] [WorldCat.org] [DOI] (P p)