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Journal of Bacteriology, March 2005, p. 1884-1891, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1884-1891.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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

Wen-Jen Yang{dagger} and Charles Yanofsky*

Department of Biological Sciences, Stanford University, Stanford, California

Received 4 November 2004/ Accepted 8 December 2004

The anti-TRAP protein (AT), encoded by the rtpA gene of Bacillus subtilis, can bind to and inhibit the tryptophan-activated trp RNA-binding attenuation protein (TRAP). AT binding can prevent TRAP from promoting transcription termination in the leader region of the trp operon, thereby increasing trp operon expression. We show here that AT levels continue to increase as tryptophan starvation becomes more severe, whereas the TRAP level remains relatively constant and independent of tryptophan starvation. Assuming that the functional form of AT is a trimer, we estimate that the ratios of AT trimers per TRAP molecule are 0.39 when the cells are grown under mild tryptophan starvation conditions, 0.83 under more severe starvation conditions, and approximately 2.0 when AT is expressed maximally. As the AT level is increased, a corresponding increase is observed in the anthranilate synthase level. When AT is expressed maximally, the anthranilate synthase level is about 70% of the level observed in a strain lacking TRAP. In a nutritional shift experiment where excess phenylalanine and tyrosine could potentially starve cells of tryptophan, both the AT level and anthranilate synthase activity were observed to increase. Expression of the trp operon is clearly influenced by the level of AT.

* Corresponding author. Mailing address: Department of Biological Sciences, Stanford University, Stanford, CA 94305. Phone: (650) 725-1835. Fax: (650) 725-8221. E-mail: yanofsky{at}cmgm.stanford.edu.

{dagger} Present address: Department of Life Sciences and Institute of Biotechnology, National University of Kaohsiung, Kaohsiung, Taiwan.

Journal of Bacteriology, March 2005, p. 1884-1891, Vol. 187, No. 6
0021-9193/05/$08.00+0     doi:10.1128/JB.187.6.1884-1891.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Cruz-Vera, L. R., Gong, M., Yanofsky, C. (2008). Physiological Effects of Anti-TRAP Protein Activity and tRNATrp Charging on trp Operon Expression in Bacillus subtilis. J. Bacteriol. 190: 1937-1945 [Abstract] [Full Text]  
  • Shevtsov, M. B., Chen, Y., Gollnick, P., Antson, A. A. (2005). Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction. Proc. Natl. Acad. Sci. USA 102: 17600-17605 [Abstract] [Full Text]  


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