RtpA

• Description: anti-TRAP
  
  

Gene name	rtpA
Synonyms	yczA
Essential	no
Product	anti-TRAP
Function	regulation of tryptophan biosynthesis
Gene expression levels in SubtiExpress: rtpA
Interactions involving this protein in SubtInteract: RtpA
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
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

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

• Expression browser: rtpA 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)