SacY

• Description: transcriptional antiterminator for sacB and sacX-sacY (acts at high sucrose concentrations)
  
  

Gene name	sacY
Synonyms	ipa-13r, sacS
Essential	no
Product	transcriptional antiterminator
Function	regulation of sucrose utilization
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism, Stress
MW, pI	32 kDa, 5.883
Gene length, protein length	840 bp, 280 aa
Immediate neighbours	sacX, gspA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU38420

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: binding to the mRNA of sacB and the sacX-sacY operon, causes transcription antitermination (in presence of sucrose)

• Protein family: transcriptional antiterminator bglG family (according to Swiss-Prot) BglG family of antiterminators

• Paralogous protein(s): LicT, GlcT, SacT

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: PtsH-SacY

• Localization:

Database entries

• Structure: 1AUU (RNA-binding domain)

• UniProt: P15401

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: sacX-sacY

• Sigma factor: SigA

• Regulation: induction by sucrose (at high concentration)

• Regulatory mechanism: induction by SacY-dependent RNA switch (transcriptional antitermination)

• Additional information:

Biological materials

• Mutant: GP425 (cat), available in Stülke lab

• Expression vector:
  • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag, in pWH844: pGP316, available in Stülke lab
  • for expression, purification of the RNA-binding domain in E. coli with N-terminal His-tag and thrombin cleavage site, in pGP570: pGP573, available in Stülke lab

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Labs working on this gene/protein

Stephane Aymerich, Microbiology and Molecular Genetics, INRA Paris-Grignon, France

References

P Tortosa, N Declerck, H Dutartre, C Lindner, J Deutscher, D Le Coq
Sites of positive and negative regulation in the Bacillus subtilis antiterminators LicT and SacY.
Mol Microbiol: 2001, 41(6);1381-93
[PubMed:11580842] [WorldCat.org] [DOI] (P p)

N Declerck, F Vincent, F Hoh, S Aymerich, H van Tilbeurgh
RNA recognition by transcriptional antiterminators of the BglG/SacY family: functional and structural comparison of the CAT domain from SacY and LicT.
J Mol Biol: 1999, 294(2);389-402
[PubMed:10610766] [WorldCat.org] [DOI] (P p)

H van Tilbeurgh, X Manival, S Aymerich, J M Lhoste, C Dumas, M Kochoyan
Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis.
EMBO J: 1997, 16(16);5030-6
[PubMed:9305644] [WorldCat.org] [DOI] (P p)

X Manival, Y Yang, M P Strub, M Kochoyan, M Steinmetz, S Aymerich
From genetic to structural characterization of a new class of RNA-binding domain within the SacY/BglG family of antiterminator proteins.
EMBO J: 1997, 16(16);5019-29
[PubMed:9305643] [WorldCat.org] [DOI] (P p)

P Tortosa, S Aymerich, C Lindner, M H Saier, J Reizer, D Le Coq
Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system.
J Biol Chem: 1997, 272(27);17230-7
[PubMed:9202047] [WorldCat.org] [DOI] (P p)

M Arnaud, M Débarbouillé, G Rapoport, M H Saier, J Reizer
In vitro reconstitution of transcriptional antitermination by the SacT and SacY proteins of Bacillus subtilis.
J Biol Chem: 1996, 271(31);18966-72
[PubMed:8702561] [WorldCat.org] [DOI] (P p)

S Aymerich, M Steinmetz
Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family.
Proc Natl Acad Sci U S A: 1992, 89(21);10410-4
[PubMed:1279678] [WorldCat.org] [DOI] (P p)

A M Crutz, M Steinmetz, S Aymerich, R Richter, D Le Coq
Induction of levansucrase in Bacillus subtilis: an antitermination mechanism negatively controlled by the phosphotransferase system.
J Bacteriol: 1990, 172(2);1043-50
[PubMed:2105292] [WorldCat.org] [DOI] (P p)