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Review
. 2001 Oct;183(20):5795-802.
doi: 10.1128/JB.183.20.5795-5802.2001.

Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure

P Babitzke  1 , P Gollnick
Affiliations
Review

Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure

P Babitzke et al. J Bacteriol. 2001 Oct.
No abstract available

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Figures

FIG. 1
FIG. 1
Folate, mtr, trp, yhaG, and yczA-ycbK operons. trpG is located within the folate operon, while the rest of the trp genes are clustered in the trpEDCFBA operon. yhaG encodes a putative tryptophan transport protein. mtrB encodes TRAP, while yczA encodes the AT protein (41). TRAP is responsible for regulating expression of the trp operon by transcription attenuation and a translational control mechanism. TRAP regulates translation of trpG, yhaG, and probably ycbK. P> marks the position of the promoters for each operon, while the black boxes show the positions of the TRAP binding sites. The positions of terminator hairpins (open circles) and antiterminator hairpins (filled circles) are shown.
FIG. 2
FIG. 2
Transcription attenuation model of the trp operon. When tryptophan is limiting (−tryptophan) TRAP is not activated. During transcription, antiterminator formation (A and B) prevents formation of the terminator (C and D), which results in transcription of the trp operon structural genes. When tryptophan is in excess (+tryptophan) TRAP is activated. Tryptophan-activated TRAP can bind to the (G/U)AG repeats and promote termination by preventing antiterminator formation. The overlap between the antiterminator and terminator structures is shown. Numbering is from the start of transcription.
FIG. 3
FIG. 3
trpE translational control model. Under tryptophan-limiting conditions, TRAP is not activated and is unable to bind to the trp leader transcript. In this case the trp leader RNA adopts a structure such that the trpE SD sequence is single stranded and available for translation. Under excess tryptophan conditions, TRAP is activated and binds to the (G/U)AG repeats. As a consequence, the trpE SD blocking hairpin forms, which prevents ribosome binding and translation. The overlap between the two alternative structures is shown. Numbering is from the start of transcription.
FIG. 4
FIG. 4
Comparison of the TRAP binding sites. The (G/U)AG repeats are shown in bold type. The positions of the SD sequences and the start codons are shown for trpG, ycbK, and yhaG.
FIG. 5
FIG. 5
Ribbon diagram of TRAP complexed with an RNA containing 11 GAG repeats separated by AU spacers. TRAP binds to the linear transcript and wraps the RNA around the periphery of the TRAP complex. The TRAP subunits are shown in various shades of gray, and the RNA is shown in ball-and-stick models. The bound l-tryptophan molecules are shown as van der Waals spheres.
See this image and copyright information in PMC

References

    1. Antson A A, Dodson E J, Dodson G, Greaves R B, Chen X, Gollnick P. Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA. Nature. 1999;401:235–242. - PubMed
    1. Antson A A, Otridge J, Brzozowski A M, Dodson E J, Dodson G G, Wilson K S, Smith T M, Yang M, Kurecki T, Gollnick P. The structure of the trp RNA attenuation protein. Nature. 1995;374:693–700. - PubMed
    1. Babitzke P. Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel. Mol Microbiol. 1997;26:1–9. - PubMed
    1. Babitzke P, Yanofsky C. Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein. Proc Natl Acad Sci USA. 1993;90:133–137. - PMC - PubMed
    1. Babitzke P, Yanofsky C. Structural features of L-tryptophan required for activation of TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis. J Biol Chem. 1995;270:12452–12456. - PubMed

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