Physiological effects of anti-TRAP protein activity and tRNA(Trp) charging on trp operon expression in Bacillus subtilis

Journal of Bacteriology
Luis R Cruz-VeraC Yanofsky

Abstract

The Bacillus subtilis anti-TRAP protein regulates the ability of the tryptophan-activated TRAP protein to bind to trp operon leader RNA and promote transcription termination. AT synthesis is regulated both transcriptionally and translationally by uncharged tRNA(Trp). In this study, we examined the roles of AT synthesis and tRNA(Trp) charging in mediating physiological responses to tryptophan starvation. Adding excess phenylalanine to wild-type cultures reduced the charged tRNA(Trp) level from 80% to 40%; the charged level decreased further, to 25%, in an AT-deficient mutant. Adding tryptophan with phenylalanine increased the charged tRNA(Trp) level, implying that phenylalanine, when added alone, reduces the availability of tryptophan for tRNA(Trp) charging. Changes in the charged tRNA(Trp) level observed during growth with added phenylalanine were associated with increased transcription of the genes of tryptophan metabolism. Nutritional shift experiments, from a medium containing tryptophan to a medium with phenylalanine and tyrosine, showed that wild-type cultures gradually reduced their charged tRNA(Trp) level. When this shift was performed with an AT-deficient mutant, the charged tRNA(Trp) level decreased even further. Growt...Continue Reading

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Citations

Aug 18, 2010·Proceedings of the National Academy of Sciences of the United States of America·Joseph R SachlebenMark P Foster
Feb 20, 2014·Proceedings of the National Academy of Sciences of the United States of America·Elihu C IhmsMark P Foster
Oct 28, 2009·Cellular and Molecular Life Sciences : CMLS·Pascale Romby, Emmanuelle Charpentier

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