RtpA

• Description: anti-TRAP
  
  

Gene name	rtpA
Synonyms	yczA
Essential	no
Product	anti-TRAP
Function	regulation of tryptophan biosynthesis
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp
MW, pI	5 kDa, 4.862
Gene length, protein length	159 bp, 53 aa
Immediate neighbours	ycbJ, ycbK
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, transcription factors and their control

This gene is a member of the following regulons

T-box

The gene

Basic information

• Locus tag: BSU02530

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions: TRAP-RtpA PubMed, forms trimers and dodecamers (tetramer of trimers) PubMed, only the trimeric form interacts with TRAP PubMed

• Localization: cytoplasm (according to Swiss-Prot)

Database entries

• Structure: 1N53 (structure of T box RNA), 2BX9, 2ZP9 (complex with MtrB)

• UniProt: O31466

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: rtpA-ycbK PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induced by tryptophan limitation (T-box in the mRNA leader, TRAP) PubMed

• Regulatory mechanism:
  • T-box, TRAP: transcription termination/ antitermination PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)

Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852] [WorldCat.org] [DOI] (P p)

Original Publications

Joseph R Sachleben, Craig A McElroy, Paul Gollnick, Mark P Foster
Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein.
Proc Natl Acad Sci U S A: 2010, 107(35);15385-90
[PubMed:20713740] [WorldCat.org] [DOI] (I p)

Yanling Chen, Paul Gollnick
Alanine scanning mutagenesis of anti-TRAP (AT) reveals residues involved in binding to TRAP.
J Mol Biol: 2008, 377(5);1529-43
[PubMed:18334255] [WorldCat.org] [DOI] (I p)

Luis R Cruz-Vera, Ming Gong, Charles Yanofsky
Physiological effects of anti-TRAP protein activity and tRNA(Trp) charging on trp operon expression in Bacillus subtilis.
J Bacteriol: 2008, 190(6);1937-45
[PubMed:18178730] [WorldCat.org] [DOI] (I p)

Mikhail B Shevtsov, Yanling Chen, Paul Gollnick, Alfred A Antson
Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction.
Proc Natl Acad Sci U S A: 2005, 102(49);17600-5
[PubMed:16306262] [WorldCat.org] [DOI] (P p)

Wen-Jen Yang, Charles Yanofsky
Effects of tryptophan starvation on levels of the trp RNA-binding attenuation protein (TRAP) and anti-TRAP regulatory protein and their influence on trp operon expression in Bacillus subtilis.
J Bacteriol: 2005, 187(6);1884-91
[PubMed:15743934] [WorldCat.org] [DOI] (P p)

Mikhail B Shevtsov, Yanling Chen, Paul Gollnick, Alfred A Antson
Anti-TRAP protein from Bacillus subtilis: crystallization and internal symmetry.
Acta Crystallogr D Biol Crystallogr: 2004, 60(Pt 7);1311-4
[PubMed:15213402] [WorldCat.org] [DOI] (P p)

Doug Snyder, Jeffrey Lary, Yanling Chen, Paul Gollnick, James L Cole
Interaction of the trp RNA-binding attenuation protein (TRAP) with anti-TRAP.
J Mol Biol: 2004, 338(4);669-82
[PubMed:15099736] [WorldCat.org] [DOI] (P p)

Guangnan Chen, Charles Yanofsky
Features of a leader peptide coding region that regulate translation initiation for the anti-TRAP protein of B. subtilis.
Mol Cell: 2004, 13(5);703-11
[PubMed:15023340] [WorldCat.org] [DOI] (P p)

Guangnan Chen, Charles Yanofsky
Tandem transcription and translation regulatory sensing of uncharged tryptophan tRNA.
Science: 2003, 301(5630);211-3
[PubMed:12855807] [WorldCat.org] [DOI] (I p)

Angela Valbuzzi, Charles Yanofsky
Zinc is required for assembly and function of the anti-trp RNA-binding attenuation protein, AT.
J Biol Chem: 2002, 277(50);48574-8
[PubMed:12386162] [WorldCat.org] [DOI] (P p)

Angela Valbuzzi, Paul Gollnick, Paul Babitzke, Charles Yanofsky
The anti-trp RNA-binding attenuation protein (Anti-TRAP), AT, recognizes the tryptophan-activated RNA binding domain of the TRAP regulatory protein.
J Biol Chem: 2002, 277(12);10608-13
[PubMed:11786553] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick
Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure.
J Bacteriol: 2001, 183(20);5795-802
[PubMed:11566976] [WorldCat.org] [DOI] (P p)

A Valbuzzi, C Yanofsky
Inhibition of the B. subtilis regulatory protein TRAP by the TRAP-inhibitory protein, AT.
Science: 2001, 293(5537);2057-9
[PubMed:11557884] [WorldCat.org] [DOI] (P p)

J P Sarsero, E Merino, C Yanofsky
A Bacillus subtilis operon containing genes of unknown function senses tRNATrp charging and regulates expression of the genes of tryptophan biosynthesis.
Proc Natl Acad Sci U S A: 2000, 97(6);2656-61
[PubMed:10706627] [WorldCat.org] [DOI] (P p)