Difference between revisions of "NusG"

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(References)
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=References=
 
=References=
 +
==Reviews==
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<pubmed> 24632072 </pubmed>
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==Original publications==
 
<pubmed>18852477 16707701 11101662 10027981 23033921,21040729,20384694 </pubmed>
 
<pubmed>18852477 16707701 11101662 10027981 23033921,21040729,20384694 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 08:52, 19 March 2014

  • Description: transcription antitermination and pausing factor

Gene name nusG
Synonyms
Essential no
Product transcription antitermination and pausing factor
Function transcription
Gene expression levels in SubtiExpress: nusG
Interactions involving this protein in SubtInteract: NusG
MW, pI 19 kDa, 5.252
Gene length, protein length 531 bp, 177 aa
Immediate neighbours secE, rplK
Sequences Protein DNA DNA_with_flanks
Genetic context
NusG context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
NusG expression.png















Categories containing this gene/protein

transcription

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU01010

Phenotypes of a mutant

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: KOW domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure:
  • KEGG entry: [2]
  • E.C. number:

Additional information

Expression and regulation

  • Operon:
  • Regulation:
    • strongly repressed in response to glucose starvation in M9 medium 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

Alexander V Yakhnin, Paul Babitzke
NusG/Spt5: are there common functions of this ubiquitous transcription elongation factor?
Curr Opin Microbiol: 2014, 18;68-71
[PubMed:24632072] [WorldCat.org] [DOI] (I p)

Original publications

Imke G de Jong, Jan-Willem Veening, Oscar P Kuipers
Single cell analysis of gene expression patterns during carbon starvation in Bacillus subtilis reveals large phenotypic variation.
Environ Microbiol: 2012, 14(12);3110-21
[PubMed:23033921] [WorldCat.org] [DOI] (I p)

Jisha Chalissery, Ghazala Muteeb, Nisha C Kalarickal, Shalini Mohan, V Jisha, Ranjan Sen
Interaction surface of the transcription terminator Rho required to form a complex with the C-terminal domain of the antiterminator NusG.
J Mol Biol: 2011, 405(1);49-64
[PubMed:21040729] [WorldCat.org] [DOI] (I p)

Alexander V Yakhnin, Paul Babitzke
Mechanism of NusG-stimulated pausing, hairpin-dependent pause site selection and intrinsic termination at overlapping pause and termination sites in the Bacillus subtilis trp leader.
Mol Microbiol: 2010, 76(3);690-705
[PubMed:20384694] [WorldCat.org] [DOI] (I p)

Alexander V Yakhnin, Helen Yakhnin, Paul Babitzke
Function of the Bacillus subtilis transcription elongation factor NusG in hairpin-dependent RNA polymerase pausing in the trp leader.
Proc Natl Acad Sci U S A: 2008, 105(42);16131-6
[PubMed:18852477] [WorldCat.org] [DOI] (I p)

Geoff P Doherty, Donna H Meredith, Peter J Lewis
Subcellular partitioning of transcription factors in Bacillus subtilis.
J Bacteriol: 2006, 188(11);4101-10
[PubMed:16707701] [WorldCat.org] [DOI] (P p)

C J Ingham, P A Furneaux
Mutations in the ss subunit of the Bacillus subtilis RNA polymerase that confer both rifampicin resistance and hypersensitivity to NusG.
Microbiology (Reading): 2000, 146 Pt 12;3041-3049
[PubMed:11101662] [WorldCat.org] [DOI] (P p)

C J Ingham, J Dennis, P A Furneaux
Autogenous regulation of transcription termination factor Rho and the requirement for Nus factors in Bacillus subtilis.
Mol Microbiol: 1999, 31(2);651-63
[PubMed:10027981] [WorldCat.org] [DOI] (P p)