CysH

• Description: phosphoadenosine phosphosulfate sulfotransferase
  
  

Gene name	cysH
Synonyms
Essential	no
Product	phosphoadenosine phosphosulfate sulfotransferase
Function	sulfate reduction
Metabolic function and regulation of this protein in SubtiPathways: Cys, Met & Sulfate assimilation
MW, pI	26 kDa, 5.462
Gene length, protein length	699 bp, 233 aa
Immediate neighbours	pyrE, cysP
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

sulfur metabolism

This gene is a member of the following regulons

CymR regulon, S-box

The gene

Basic information

• Locus tag: BSU15570

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin (according to Swiss-Prot)

• Protein family: CysH subfamily (according to Swiss-Prot)

• Paralogous protein(s): YitB

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• Structure:

• UniProt: P94498

• KEGG entry: [3]

• E.C. number: 1.8.4.8

Expression and regulation

• Operon: cysH-cysP-sat-cysC-ylnD-ylnE-ylnF PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by casamino acids PubMed
  • repressed in the presence of cysteine (CymR)
  • induced by methionine starvation (S-box) PubMed

• Regulatory mechanism:
  • S-box: transcription termination/ antitermination, the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed
  • CymR: transcription repression

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Isabelle Martin-Verstraete, Institute Pasteur, Paris, France

References

Jerneja Tomsic, Brooke A McDaniel, Frank J Grundy, Tina M Henkin
Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro.
J Bacteriol: 2008, 190(3);823-33
[PubMed:18039762] [WorldCat.org] [DOI] (I p)

Daniela Albanesi, Maria Cecilia Mansilla, Gustavo E Schujman, Diego de Mendoza
Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation.
J Bacteriol: 2005, 187(22);7631-8
[PubMed:16267287] [WorldCat.org] [DOI] (P p)

Ulrike Mäder, Georg Homuth, Christian Scharf, Knut Büttner, Rüdiger Bode, Michael Hecker
Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability.
J Bacteriol: 2002, 184(15);4288-95
[PubMed:12107147] [WorldCat.org] [DOI] (P p)

M C Mansilla, D Albanesi, D de Mendoza
Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis.
J Bacteriol: 2000, 182(20);5885-92
[PubMed:11004190] [WorldCat.org] [DOI] (P p)

F J Grundy, T M Henkin
The S box regulon: a new global transcription termination control system for methionine and cysteine biosynthesis genes in gram-positive bacteria.
Mol Microbiol: 1998, 30(4);737-49
[PubMed:10094622] [WorldCat.org] [DOI] (P p)

M C Mansilla, D de Mendoza
L-cysteine biosynthesis in Bacillus subtilis: identification, sequencing, and functional characterization of the gene coding for phosphoadenylylsulfate sulfotransferase.
J Bacteriol: 1997, 179(3);976-81
[PubMed:9006060] [WorldCat.org] [DOI] (P p)