Document Detail


A Bacillus subtilis operon containing genes of unknown function senses tRNATrp charging and regulates expression of the genes of tryptophan biosynthesis.
MedLine Citation:
PMID:  10706627     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Strains of Bacillus subtilis containing a temperature-sensitive tryptophanyl-tRNA synthetase produce elevated levels of the tryptophan pathway enzymes, when grown at high temperatures in the presence of excess tryptophan. This increase is because of reduced availability of the tryptophan-activated trp RNA-binding attenuation protein (TRAP). To test the hypothesis that this elevated trp gene expression was caused by the overproduction of a transcript capable of binding and sequestering TRAP, a computer program was designed to search the B. subtilis genome sequence for additional potential TRAP binding sites. A region containing a stretch of (G/A)AG trinucleotide repeats, characteristic of a TRAP binding site, was identified in the yczA-ycbK operon. We show that transcriptional regulation of the yczA-ycbK operon is controlled by the T-box antitermination mechanism in response to the level of uncharged tRNA(Trp), and that the presence of a trpS1 mutant allele increases production of the yczA-ycbK transcript. Elevated yczA-ycbK expression was shown to activate transcription of the trp operon. Deletion of the yczA-ycbK operon abolishes the trpS1 effect on trp gene expression. The purpose of increasing expression of the genes of tryptophan biosynthesis in the trpS mutant would be to provide additional tryptophan to overcome the charged tRNA(Trp) deficiency. Therefore, in B. subtilis, as in Escherichia coli, transcription of the tryptophan biosynthetic genes is regulated in response to changes in the extent of charging of tRNA(Trp) as well as the availability of tryptophan.
Authors:
J P Sarsero; E Merino; C Yanofsky
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Proceedings of the National Academy of Sciences of the United States of America     Volume:  97     ISSN:  0027-8424     ISO Abbreviation:  Proc. Natl. Acad. Sci. U.S.A.     Publication Date:  2000 Mar 
Date Detail:
Created Date:  2000-04-25     Completed Date:  2000-04-25     Revised Date:  2013-04-16    
Medline Journal Info:
Nlm Unique ID:  7505876     Medline TA:  Proc Natl Acad Sci U S A     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  2656-61     Citation Subset:  IM    
Affiliation:
Department of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA.
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MeSH Terms
Descriptor/Qualifier:
Anthranilate Synthase*
Bacillus subtilis / genetics*
Base Sequence
Binding Sites
Chromosome Deletion
Computer Simulation
Gene Deletion
Gene Expression Regulation, Bacterial*
Molecular Sequence Data
Nitrogenous Group Transferases / genetics
Nucleic Acid Conformation
Operon*
RNA, Transfer, Amino Acyl / metabolism*
Trans-Activators / genetics
Transcription, Genetic
Tryptophan / biosynthesis*,  genetics*
Grant Support
ID/Acronym/Agency:
GM09738/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/RNA, Transfer, Amino Acyl; 0/Trans-Activators; 73-22-3/Tryptophan; EC 2.6.-/Nitrogenous Group Transferases; EC 4.1.3.27/Anthranilate Synthase; EC 4.1.3.27/anthranilate synthase, glutamine amidotransferase subunit
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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