Inhibition of the B. subtilis Regulatory Protein TRAP by the TRAP-Inhibitory Protein, AT

Autor:	Angela Valbuzzi, Charles Yanofsky
Rok vydání:	2001
Předmět:	Transcription Genetic Operon Amino Acid Motifs Molecular Sequence Data Bacillus subtilis Biology trp operon Bacterial Proteins Transcription (biology) Gene expression Amino Acid Sequence Multidisciplinary Tryptophan RNA-Binding Proteins RNA Gene Expression Regulation Bacterial RNA Transfer Trp biology.organism_classification RNA Bacterial Cross-Linking Reagents Biochemistry Glutaral Transfer RNA Electrophoresis Polyacrylamide Gel 5' Untranslated Regions Sequence Alignment Transcription Factors
Zdroj:	Science. 293:2057-2059
ISSN:	1095-9203 0036-8075
DOI:	10.1126/science.1062187
Popis:	An anti-TRAP (AT) protein, a factor of previously unknown function, conveys the metabolic signal that the cellular transfer RNA for tryptophan (tRNA Trp ) is predominantly uncharged. Expression of the operon encoding AT is induced by uncharged tRNA Trp . AT associates with TRAP, the trp operon attenuation protein, and inhibits its binding to its target RNA sequences. This relieves TRAP-mediated transcription termination and translation inhibition, increasing the rate of tryptophan biosynthesis. AT binds to TRAP primarily when it is in the tryptophan-activated state. The 53-residue AT polypeptide is homologous to the zinc-binding domain of DnaJ. The mechanisms regulating tryptophan biosynthesis in Bacillus subtilis differ from those used by Escherichia coli .
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d07f4af702f29483bc86cc31379b799 https://doi.org/10.1126/science.1062187 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
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