MtrB

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  • Description: tryptophan operon RNA-binding attenuation protein (TRAP), controls the RNA switch in front of genes involved in biosynthesis and acquisition of tryptophan

Gene name mtrB
Synonyms
Essential no
Product tryptophan operon RNA-binding attenuation protein (TRAP)
Function regulation of tryptophan biosynthesis
(and translation) attenuation in the trp operon;
repression of the folate operon
Interactions involving this protein in SubtInteract: TRAP
Metabolic function and regulation of this protein in SubtiPathways:
Phe, Tyr, Trp, Folate
MW, pI 8 kDa, 7.333
Gene length, protein length 225 bp, 75 aa
Immediate neighbours hepS, folE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
MtrB context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

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

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU22770

Expression

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: prpD family (according to Swiss-Prot)
  • Paralogous protein(s):

Genes controlled by MtrB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
    • binding of tryptophan results RNA binding and thus in transcription termination

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Original Publications

Chao-Sheng Chen, Callum Smits, Guy G Dodson, Mikhail B Shevtsov, Natalie Merlino, Paul Gollnick, Alfred A Antson
How to change the oligomeric state of a circular protein assembly: switch from 11-subunit to 12-subunit TRAP suggests a general mechanism.
PLoS One: 2011, 6(10);e25296
[PubMed:21984911] [WorldCat.org] [DOI] (I p)

Kristine D Potter, Natalie M Merlino, Timothy Jacobs, Paul Gollnick
TRAP binding to the Bacillus subtilis trp leader region RNA causes efficient transcription termination at a weak intrinsic terminator.
Nucleic Acids Res: 2011, 39(6);2092-102
[PubMed:21097886] [WorldCat.org] [DOI] (I p)

Adam P McGraw, Ali Mokdad, François Major, Philip C Bevilacqua, Paul Babitzke
Molecular basis of TRAP-5'SL RNA interaction in the Bacillus subtilis trp operon transcription attenuation mechanism.
RNA: 2009, 15(1);55-66
[PubMed:19033375] [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)

Adam P McGraw, Philip C Bevilacqua, Paul Babitzke
TRAP-5' stem loop interaction increases the efficiency of transcription termination in the Bacillus subtilis trpEDCFBA operon leader region.
RNA: 2007, 13(11);2020-33
[PubMed:17881743] [WorldCat.org] [DOI] (P p)

Maria V Barbolina, Roman Kristoforov, Amanda Manfredo, Yanling Chen, Paul Gollnick
The rate of TRAP binding to RNA is crucial for transcription attenuation control of the B. subtilis trp operon.
J Mol Biol: 2007, 370(5);925-38
[PubMed:17555767] [WorldCat.org] [DOI] (P p)

Helen Yakhnin, Alexander V Yakhnin, Paul Babitzke
Translation control of trpG from transcripts originating from the folate operon promoter of Bacillus subtilis is influenced by translation-mediated displacement of bound TRAP, while translation control of transcripts originating from a newly identified trpG promoter is not.
J Bacteriol: 2007, 189(3);872-9
[PubMed:17114263] [WorldCat.org] [DOI] (P p)

Alexander V Yakhnin, Helen Yakhnin, Paul Babitzke
RNA polymerase pausing regulates translation initiation by providing additional time for TRAP-RNA interaction.
Mol Cell: 2006, 24(4);547-57
[PubMed:17114058] [WorldCat.org] [DOI] (P p)

Helen Yakhnin, Alexander V Yakhnin, Paul Babitzke
The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis regulates translation initiation of ycbK, a gene encoding a putative efflux protein, by blocking ribosome binding.
Mol Microbiol: 2006, 61(5);1252-66
[PubMed:16879415] [WorldCat.org] [DOI] (P p)

Craig A McElroy, Amanda Manfredo, Paul Gollnick, Mark P Foster
Thermodynamics of tryptophan-mediated activation of the trp RNA-binding attenuation protein.
Biochemistry: 2006, 45(25);7844-53
[PubMed:16784236] [WorldCat.org] [DOI] (P p)

Vandana Payal, Paul Gollnick
Substitutions of Thr30 provide mechanistic insight into tryptophan-mediated activation of TRAP binding to RNA.
Nucleic Acids Res: 2006, 34(10);2933-42
[PubMed:16738132] [WorldCat.org] [DOI] (I e)

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)

Maria V Barbolina, Xiufeng Li, Paul Gollnick
Bacillus subtilis TRAP binds to its RNA target by a 5' to 3' directional mechanism.
J Mol Biol: 2005, 345(4);667-79
[PubMed:15588817] [WorldCat.org] [DOI] (P p)

Barbara C McCabe, Paul Gollnick
Cellular levels of trp RNA-binding attenuation protein in Bacillus subtilis.
J Bacteriol: 2004, 186(15);5157-9
[PubMed:15262953] [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)

Nicholas H Hopcroft, Amanda Manfredo, Alice L Wendt, Andrzej M Brzozowski, Paul Gollnick, Alfred A Antson
The interaction of RNA with TRAP: the role of triplet repeats and separating spacer nucleotides.
J Mol Biol: 2004, 338(1);43-53
[PubMed:15050822] [WorldCat.org] [DOI] (P p)

Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255] [WorldCat.org] [DOI] (P p)

Helen Yakhnin, Hong Zhang, Alexander V Yakhnin, Paul Babitzke
The trp RNA-binding attenuation protein of Bacillus subtilis regulates translation of the tryptophan transport gene trpP (yhaG) by blocking ribosome binding.
J Bacteriol: 2004, 186(2);278-86
[PubMed:14702295] [WorldCat.org] [DOI] (P p)

Pan T X Li, Paul Gollnick
Characterization of a trp RNA-binding attenuation protein (TRAP) mutant with tryptophan independent RNA binding activity.
J Mol Biol: 2004, 335(3);707-22
[PubMed:14687568] [WorldCat.org] [DOI] (P p)

Janell E Schaak, Helen Yakhnin, Philip C Bevilacqua, Paul Babitzke
A Mg2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding.
J Mol Biol: 2003, 332(3);555-74
[PubMed:12963367] [WorldCat.org] [DOI] (P p)

Pan T X Li, Paul Gollnick
Using hetero-11-mers composed of wild type and mutant subunits to study tryptophan binding to TRAP and its role in activating RNA binding.
J Biol Chem: 2002, 277(38);35567-73
[PubMed:12133840] [WorldCat.org] [DOI] (P p)

Nicholas H Hopcroft, Alice L Wendt, Paul Gollnick, Alfred A Antson
Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences.
Acta Crystallogr D Biol Crystallogr: 2002, 58(Pt 4);615-21
[PubMed:11914485] [WorldCat.org] [DOI] (P p)

Pan T X Li, David J Scott, Paul Gollnick
Creating hetero-11-mers composed of wild-type and mutant subunits to study RNA binding to TRAP.
J Biol Chem: 2002, 277(14);11838-44
[PubMed:11805104] [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)

M B Elliott, P A Gottlieb, P Gollnick
The mechanism of RNA binding to TRAP: initiation and cooperative interactions.
RNA: 2001, 7(1);85-93
[PubMed:11214184] [WorldCat.org] [DOI] (P p)

J P Sarsero, E Merino, C Yanofsky
A Bacillus subtilis gene of previously unknown function, yhaG, is translationally regulated by tryptophan-activated TRAP and appears to be involved in tryptophan transport.
J Bacteriol: 2000, 182(8);2329-31
[PubMed:10735881] [WorldCat.org] [DOI] (P p)

H Du, A V Yakhnin, S Dharmaraj, P Babitzke
trp RNA-binding attenuation protein-5' stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon.
J Bacteriol: 2000, 182(7);1819-27
[PubMed:10714985] [WorldCat.org] [DOI] (P p)

A V Yakhnin, J J Trimble, C R Chiaro, P Babitzke
Effects of mutations in the L-tryptophan binding pocket of the Trp RNA-binding attenuation protein of Bacillus subtilis.
J Biol Chem: 2000, 275(6);4519-24
[PubMed:10660627] [WorldCat.org] [DOI] (P p)

A A Antson, E J Dodson, G Dodson, R B Greaves, X Chen, P Gollnick
Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA.
Nature: 1999, 401(6750);235-42
[PubMed:10499579] [WorldCat.org] [DOI] (P p)

X p Chen, A A Antson, M Yang, P Li, C Baumann, E J Dodson, G G Dodson, P Gollnick
Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus.
J Mol Biol: 1999, 289(4);1003-16
[PubMed:10369778] [WorldCat.org] [DOI] (P p)

S Xirasagar, M B Elliott, W Bartolini, P Gollnick, P A Gottlieb
RNA structure inhibits the TRAP (trp RNA-binding attenuation protein)-RNA interaction.
J Biol Chem: 1998, 273(42);27146-53
[PubMed:9765233] [WorldCat.org] [DOI] (P p)

C Baumann, S Xirasagar, P Gollnick
The trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis binds to unstacked trp leader RNA.
J Biol Chem: 1997, 272(32);19863-9
[PubMed:9242649] [WorldCat.org] [DOI] (P p)

M Yang, X p Chen, K Militello, R Hoffman, B Fernandez, C Baumann, P Gollnick
Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding.
J Mol Biol: 1997, 270(5);696-710
[PubMed:9245598] [WorldCat.org] [DOI] (P p)

A I Lee, J P Sarsero, C Yanofsky
A temperature-sensitive trpS mutation interferes with trp RNA-binding attenuation protein (TRAP) regulation of trp gene expression in Bacillus subtilis.
J Bacteriol: 1996, 178(22);6518-24
[PubMed:8932308] [WorldCat.org] [DOI] (P p)

C Baumann, J Otridge, P Gollnick
Kinetic and thermodynamic analysis of the interaction between TRAP (trp RNA-binding attenuation protein) of Bacillus subtilis and trp leader RNA.
J Biol Chem: 1996, 271(21);12269-74
[PubMed:8647825] [WorldCat.org] [DOI] (P p)

P Babitzke, D G Bear, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides.
Proc Natl Acad Sci U S A: 1995, 92(17);7916-20
[PubMed:7544009] [WorldCat.org] [DOI] (P p)

P Babitzke, C Yanofsky
Structural features of L-tryptophan required for activation of TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis.
J Biol Chem: 1995, 270(21);12452-6
[PubMed:7759487] [WorldCat.org] [DOI] (P p)

A A Antson, J Otridge, A M Brzozowski, E J Dodson, G G Dodson, K S Wilson, T M Smith, M Yang, T Kurecki, P Gollnick
The structure of trp RNA-binding attenuation protein.
Nature: 1995, 374(6524);693-700
[PubMed:7715723] [WorldCat.org] [DOI] (P p)

P Gollnick, C Baumann, M Yang, J Otridge, A Antson
Interaction of the 11-subunit trp RNA-binding attenuation protein (TRAP) with its RNA target.
Nucleic Acids Symp Ser: 1995, (33);43-5
[PubMed:8643393] [WorldCat.org] (P p)

A A Antson, A M Brzozowski, E J Dodson, Z Dauter, K S Wilson, T Kurecki, J Otridge, P Gollnick
11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis.
J Mol Biol: 1994, 244(1);1-5
[PubMed:7525975] [WorldCat.org] [DOI] (P p)

P Babitzke, J T Stults, S J Shire, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts.
J Biol Chem: 1994, 269(24);16597-604
[PubMed:7515880] [WorldCat.org] (P p)

P Babitzke, C Yanofsky
Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein.
Proc Natl Acad Sci U S A: 1993, 90(1);133-7
[PubMed:7678334] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

P Gollnick, S Ishino, M I Kuroda, D J Henner, C Yanofsky
The mtr locus is a two-gene operon required for transcription attenuation in the trp operon of Bacillus subtilis.
Proc Natl Acad Sci U S A: 1990, 87(22);8726-30
[PubMed:2123343] [WorldCat.org] [DOI] (P p)

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