NusA

• Description: transcription termination factor of RNA polymerase
  
  

Gene name	nusA
Synonyms
Essential	yes PubMed
Product	transcription termination factor
Function	transcription
Gene expression levels in SubtiExpress: nusA
Interactions involving this protein in SubtInteract: NusA
MW, pI	41 kDa, 4.583
Gene length, protein length	1113 bp, 371 aa
Immediate neighbours	ylxS, ylxR
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

transcription, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU16600

Phenotypes of a mutant

essential PubMed

Database entries

• BsubCyc: BSU16600

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family: nusA family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • NusA-RpoB PubMed

• Localization:

Database entries

• BsubCyc: BSU16600

• Structure:

• UniProt: P32727

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: ylxS-nusA-ylxR-ylxQ-infB-ylxP-rbfA PubMed

• Expression browser: nusA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1529 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 6765 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2729 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1835 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1832 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab

• Antibody:

References

Additional publications: PubMed

Xiao Yang, Seeseei Molimau, Geoff P Doherty, Elecia B Johnston, Jon Marles-Wright, Rosalba Rothnagel, Ben Hankamer, Richard J Lewis, Peter J Lewis
The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA.
EMBO Rep: 2009, 10(9);997-1002
[PubMed:19680289] [WorldCat.org] [DOI] (I p)

Karen M Davies, Amy J Dedman, Stephanie van Horck, Peter J Lewis
The NusA:RNA polymerase ratio is increased at sites of rRNA synthesis in Bacillus subtilis.
Mol Microbiol: 2005, 57(2);366-79
[PubMed:15978071] [WorldCat.org] [DOI] (P p)

Alexander V Yakhnin, Paul Babitzke
NusA-stimulated RNA polymerase pausing and termination participates in the Bacillus subtilis trp operon attenuation mechanism invitro.
Proc Natl Acad Sci U S A: 2002, 99(17);11067-72
[PubMed:12161562] [WorldCat.org] [DOI] (P p)

Christine Eymann, Georg Homuth, Christian Scharf, Michael Hecker
Bacillus subtilis functional genomics: global characterization of the stringent response by proteome and transcriptome analysis.
J Bacteriol: 2002, 184(9);2500-20
[PubMed:11948165] [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)

K Shazand, J Tucker, M Grunberg-Manago, J C Rabinowitz, T Leighton
Similar organization of the nusA-infB operon in Bacillus subtilis and Escherichia coli.
J Bacteriol: 1993, 175(10);2880-7
[PubMed:8491709] [WorldCat.org] [DOI] (P p)