| A Bacillus subtilis operon containing genes of unknown function senses tRNATrp charging and regulates expression of the genes of tryptophan biosynthesis. | |
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MedLine Citation:
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PMID: 10706627 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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J P Sarsero; E Merino; C Yanofsky |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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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:
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Created Date: 2000-04-25 Completed Date: 2000-04-25 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 7505876 Medline TA: Proc Natl Acad Sci U S A Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 2656-61 Citation Subset: IM |
Affiliation:
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Department of Biological Sciences, Stanford University, Stanford, CA 94305-5020, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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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:
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GM09738/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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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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