메뉴 건너뛰기




Volumn 186, Issue 2, 2004, Pages 278-286

The trp RNA-Binding Attenuation Protein of Bacillus subtilis Regulates Translation of the Tryptophan Transport Gene trpP (yhaG) by Blocking Ribosome Binding

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; BACTERIAL PROTEIN; CARRIER PROTEIN; GENE PRODUCT; GUANINE; PROTEIN PABA; PROTEIN TRPP; TRYPTOPHAN; TRYPTOPHAN RNA BINDING ATTENUATION PROTEIN; UNCLASSIFIED DRUG; URIDINE;

EID: 0347915671     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.186.2.278-286.2004     Document Type: Article
Times cited : (56)

References (43)
  • 1
    • 0033575897 scopus 로고    scopus 로고
    • Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA
    • Antson, A. A., E. J. Dodson, G. Dodson, R. B. Greaves, X. Chen, and P. Gollnick. 1999. Structure of the trp RNA-binding attenuation protein, TRAP. bound to RNA. Nature 401:235-242.
    • (1999) Nature , vol.401 , pp. 235-242
    • Antson, A.A.1    Dodson, E.J.2    Dodson, G.3    Greaves, R.B.4    Chen, X.5    Gollnick, P.6
  • 3
    • 0027458419 scopus 로고
    • Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein
    • Babitzke, P., and C. Yanofsky. 1993. Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein. Proc. Natl. Acad. Sci. USA 90:133-137.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 133-137
    • Babitzke, P.1    Yanofsky, C.2
  • 4
    • 0034810138 scopus 로고    scopus 로고
    • Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure
    • Babitzke, P., and P. Gollnick. 2001. Posttranscription initiation control of tryptophan metabolism in Bacillus subtilis by the trp RNA-binding attenuation protein (TRAP), anti-TRAP, and RNA structure. J. Bacteriol. 183:5795-5802.
    • (2001) J. Bacteriol. , vol.183 , pp. 5795-5802
    • Babitzke, P.1    Gollnick, P.2
  • 5
    • 0029150031 scopus 로고
    • TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides
    • Babitzke, P., D. G. Bear, and C. Yanofsky. 1995. TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a toroid-shaped molecule that binds transcripts containing GAG or UAG repeats separated by two nucleotides. Proc. Natl. Acad. Sci. USA 92:7916-7920.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7916-7920
    • Babitzke, P.1    Bear, D.G.2    Yanofsky, C.3
  • 6
    • 85058724121 scopus 로고    scopus 로고
    • Role of RNA structure in transcription attenuation in Bacillus subtilis: The trpEDCFBA operon as a model system
    • in press
    • Babitzke, P., J. Schaak, A. V. Yakhnin, and P. C. Bevilacqua. Role of RNA structure in transcription attenuation in Bacillus subtilis: the trpEDCFBA operon as a model system. Methods Enzmol., in press.
    • Methods Enzmol.
    • Babitzke, P.1    Schaak, J.2    Yakhnin, A.V.3    Bevilacqua, P.C.4
  • 7
    • 0028361572 scopus 로고
    • RAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts
    • Babitzke, P., J. T. Stults, S. J. Shire, and C. Yanofsky. 1994. RAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts. J. Biol. Chem. 269:16597-16604.
    • (1994) J. Biol. Chem. , vol.269 , pp. 16597-16604
    • Babitzke, P.1    Stults, J.T.2    Shire, S.J.3    Yanofsky, C.4
  • 8
    • 0029839067 scopus 로고    scopus 로고
    • Interaction of the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis with RNA: Effects of the number of GAG repeats, the nucleotides separating adjacent repeats, and RNA secondary structure
    • Babitzke, P., J. Yealy, and D. Campanelli. 1996. Interaction of the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis with RNA: effects of the number of GAG repeats, the nucleotides separating adjacent repeats, and RNA secondary structure. J. Bacteriol. 178:5159-5163.
    • (1996) J. Bacteriol. , vol.178 , pp. 5159-5163
    • Babitzke, P.1    Yealy, J.2    Campanelli, D.3
  • 9
    • 0026560384 scopus 로고
    • The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis
    • Babitzke, P., P. Gollnick, and C. Yanofsky. 1992. The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis. J. Bacteriol. 174:2059-2064.
    • (1992) J. Bacteriol. , vol.174 , pp. 2059-2064
    • Babitzke, P.1    Gollnick, P.2    Yanofsky, C.3
  • 10
    • 0036016824 scopus 로고    scopus 로고
    • CsrA regulates glycogen biosynthesis by preventing translation of glgC in Escherichia coli
    • Baker, C. S., I. Morozov, K. Suzuki, T. Romeo, and P. Babitzke. 2002. CsrA regulates glycogen biosynthesis by preventing translation of glgC in Escherichia coli. Mol. Microbiol. 44:1599-1610.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1599-1610
    • Baker, C.S.1    Morozov, I.2    Suzuki, K.3    Romeo, T.4    Babitzke, P.5
  • 11
    • 0030789279 scopus 로고    scopus 로고
    • The trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis binds to unstacked trp leader RNA
    • Baumann, C., S. Xirsagar, and P. Gollnick. 1997. The trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis binds to unstacked trp leader RNA. J. Biol. Chem. 272:19863-19869.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19863-19869
    • Baumann, C.1    Xirsagar, S.2    Gollnick, P.3
  • 13
    • 0037477478 scopus 로고    scopus 로고
    • Tandem transcription and translation regulatory sensing of uncharged tryptophan tRNA
    • Chen, G., and C. Yanofsky. 2003. Tandem transcription and translation regulatory sensing of uncharged tryptophan tRNA. Science 301:211-213.
    • (2003) Science , vol.301 , pp. 211-213
    • Chen, G.1    Yanofsky, C.2
  • 14
    • 0032493809 scopus 로고    scopus 로고
    • trp-RNA binding attenuation protein-mediated long-distance RNA refolding regulates translation of trpE in Bacillus subtilis
    • Du, H., and P. Babitzke. 1998. trp-RNA binding attenuation protein-mediated long-distance RNA refolding regulates translation of trpE in Bacillus subtilis. J. Biol. Chem. 273:20494-20503.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20494-20503
    • Du, H.1    Babitzke, P.2
  • 15
    • 0034022875 scopus 로고    scopus 로고
    • trp RNA-binding attenuation protein-5′ stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon
    • Du, H., A. V. Yakhnin, S. Dharmaraj, and P. Babitzke. 2000. trp RNA-binding attenuation protein-5′ stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon. J. Bacteriol. 182:1819-1827.
    • (2000) J. Bacteriol. , vol.182 , pp. 1819-1827
    • Du, H.1    Yakhnin, A.V.2    Dharmaraj, S.3    Babitzke, P.4
  • 16
    • 0030934761 scopus 로고    scopus 로고
    • The trp-RNA binding attenuation protein regulates TrpG synthesis by binding to the trpG ribosome binding site of Bacillus subtilis
    • Du, H., R. Tarpey, and P. Babitzke. 1997. The trp-RNA binding attenuation protein regulates TrpG synthesis by binding to the trpG ribosome binding site of Bacillus subtilis. J. Bacteriol. 179:2582-2586.
    • (1997) J. Bacteriol. , vol.179 , pp. 2582-2586
    • Du, H.1    Tarpey, R.2    Babitzke, P.3
  • 17
    • 0003221794 scopus 로고    scopus 로고
    • Aromatic amino acid metabolism in Bacillus subtilis
    • A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.). American Society for Microbiology, Washington, D.C.
    • Gollnick, P., P. Babitzke, E. Merino, and C. Yanofsky. 2002. Aromatic amino acid metabolism in Bacillus subtilis. p. 233-244. In A. L. Sonenshein, J. A. Hoch, and R. Losick (ed.), Bacillus subtilis and its close relatives: from genes to cells. American Society for Microbiology, Washington, D.C.
    • (2002) Bacillus Subtilis and Its Close Relatives: From Genes to Cells , pp. 233-244
    • Gollnick, P.1    Babitzke, P.2    Merino, E.3    Yanofsky, C.4
  • 18
    • 0012567905 scopus 로고    scopus 로고
    • The T box and S box transcription termination control systems
    • Grundy, F. J., and T. M. Henkin. 2003. The T box and S box transcription termination control systems. Front. Biosci. 8:20-31.
    • (2003) Front. Biosci. , vol.8 , pp. 20-31
    • Grundy, F.J.1    Henkin, T.M.2
  • 19
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz, D., D. S. McPheeters, R. Traut, and L. Gold. 1988. Extension inhibition analysis of translation initiation complexes. Methods Enzymol. 164:419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4
  • 20
    • 0028906665 scopus 로고
    • The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis
    • Hoffman, R. J., and P. Gollnick. 1995. The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis. J. Bacteriol. 177:839-842.
    • (1995) J. Bacteriol. , vol.177 , pp. 839-842
    • Hoffman, R.J.1    Gollnick, P.2
  • 21
    • 0017696790 scopus 로고
    • Regulation of a common amidotransferase subunit
    • Kane, J. F. 1977. Regulation of a common amidotransferase subunit. J. Bacteriol. 132:419-425.
    • (1977) J. Bacteriol. , vol.132 , pp. 419-425
    • Kane, J.F.1
  • 22
    • 0024041531 scopus 로고
    • cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon
    • Kuroda, M. I., D. Henner, and C. Yanofsky. 1988. cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon. J. Bacteriol. 170:3080-3088.
    • (1988) J. Bacteriol. , vol.170 , pp. 3080-3088
    • Kuroda, M.I.1    Henner, D.2    Yanofsky, C.3
  • 23
    • 0033591465 scopus 로고    scopus 로고
    • Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure
    • Mathews, D. H., J. Sabina, M. Zuker, and D. H. Turner. 1999. Expanded sequence dependence of thermodynamic parameters improves prediction of RNA secondary structure. J. Mol. Biol. 288:911-940.
    • (1999) J. Mol. Biol. , vol.288 , pp. 911-940
    • Mathews, D.H.1    Sabina, J.2    Zuker, M.3    Turner, D.H.4
  • 24
    • 0028871292 scopus 로고
    • trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon
    • Merino, E., P. Babitzke, and C. Yanofsky. 1995. trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon. J. Bacteriol. 177:6362-6370.
    • (1995) J. Bacteriol. , vol.177 , pp. 6362-6370
    • Merino, E.1    Babitzke, P.2    Yanofsky, C.3
  • 25
    • 0003785155 scopus 로고
    • Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Miller, J. 1972. Experiments in molecular genetics, p. 352-355. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1972) Experiments in Molecular Genetics , pp. 352-355
    • Miller, J.1
  • 26
    • 0027509047 scopus 로고
    • MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner
    • Otridge, J., and P. Gollnick. 1993. MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner. Proc. Natl. Acad. Sci. USA 90:128-132.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 128-132
    • Otridge, J.1    Gollnick, P.2
  • 27
    • 0034115502 scopus 로고    scopus 로고
    • A Bacillus subtilis gene of previously unknown function, yhaG, is translationally regulated by tryptophan-activated TRAP and appears to be involved in tryptophan transport
    • Sarsero, J. P., E. Merino, and C. Yanofsky. 2000. A Bacillus subtilis gene of previously unknown function, yhaG, is translationally regulated by tryptophan-activated TRAP and appears to be involved in tryptophan transport. J. Bacteriol. 182:2329-2331.
    • (2000) J. Bacteriol. , vol.182 , pp. 2329-2331
    • Sarsero, J.P.1    Merino, E.2    Yanofsky, C.3
  • 29
    • 0042736855 scopus 로고    scopus 로고
    • 2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding
    • 2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding. J. Mol. Biol. 332:555-574.
    • (2003) J. Mol. Biol. , vol.332 , pp. 555-574
    • Schaak, J.1    Yakhnin, H.2    Bevilacqua, P.C.3    Babitzke, P.4
  • 30
    • 0016436466 scopus 로고
    • Genes affecting the productivity of α-amylase in Bacillus subtilis Marburg
    • Sekiguchi, J., N. Takada, and H. Okada. 1975. Genes affecting the productivity of α-amylase in Bacillus subtilis Marburg. J. Bacteriol. 121:688-694.
    • (1975) J. Bacteriol. , vol.121 , pp. 688-694
    • Sekiguchi, J.1    Takada, N.2    Okada, H.3
  • 31
    • 0025602271 scopus 로고
    • An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene
    • Slock, J., D. P. Stahly, C.-Y. Han, E. W. Six, and I. P. Crawford. 1990. An apparent Bacillus subtilis folic acid biosynthetic operon containing pab, an amphibolic trpG gene, a third gene required for synthesis of para-aminobenzoic acid, and the dihydropteroate synthase gene. J. Bacteriol. 172:7211-7226.
    • (1990) J. Bacteriol. , vol.172 , pp. 7211-7226
    • Slock, J.1    Stahly, D.P.2    Han, C.-Y.3    Six, E.W.4    Crawford, I.P.5
  • 32
    • 0032882591 scopus 로고    scopus 로고
    • A 5′ RNA stem-loop participates in the transcription attenuation mechanism that controls expression of the Bacillus subtilis trpEDCFBA operon
    • Sudershana, S., H. Du, M. Mahalanabis, and P. Babitzke. 1999. A 5′ RNA stem-loop participates in the transcription attenuation mechanism that controls expression of the Bacillus subtilis trpEDCFBA operon. J. Bacteriol. 181:5742-5749.
    • (1999) J. Bacteriol. , vol.181 , pp. 5742-5749
    • Sudershana, S.1    Du, H.2    Mahalanabis, M.3    Babitzke, P.4
  • 33
    • 0035860533 scopus 로고    scopus 로고
    • Inhibition of TRAP, the B. subtilis trp RNA-binding attenuation protein, by the anti-TRAP protein, AT
    • Valbuzzi, A., and C. Yanofsky. 2001. Inhibition of TRAP, the B. subtilis trp RNA-binding attenuation protein, by the anti-TRAP protein, AT. Science 293:2057-2059.
    • (2001) Science , vol.293 , pp. 2057-2059
    • Valbuzzi, A.1    Yanofsky, C.2
  • 34
    • 0037073774 scopus 로고    scopus 로고
    • Zinc is required for assembly and function of the anti-trp RNA-binding attenuation protein, AT
    • Valbuzzi, A., and C. Yanofsky. 2002. Zinc is required for assembly and function of the anti-trp RNA-binding attenuation protein, AT. J. Biol. Chem. 277:48574-48578.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48574-48578
    • Valbuzzi, A.1    Yanofsky, C.2
  • 35
    • 0037155838 scopus 로고    scopus 로고
    • The anti-trp RNA-binding attenuation protein (anti-TRAP) AT, recognizes the tryptophan-activated RNA binding domain of the TRAP regulatory protein
    • Valbuzzi, A., P. Gollnick, P. Babitzke, and C. Yanofsky. 2002. The anti-trp RNA-binding attenuation protein (anti-TRAP), AT, recognizes the tryptophan-activated RNA binding domain of the TRAP regulatory protein. J. Biol. Chem. 277:10608-10613.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10608-10613
    • Valbuzzi, A.1    Gollnick, P.2    Babitzke, P.3    Yanofsky, C.4
  • 36
    • 0027172789 scopus 로고
    • A double-filter method for nitrocellulose-filter binding: Application to protein-nucleic acid interactions
    • Wong, I., and T. M. Lohman. 1993. A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions. Proc. Natl. Acad. Sci. USA 90:5428-5432.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5428-5432
    • Wong, I.1    Lohman, T.M.2
  • 37
    • 0032538567 scopus 로고    scopus 로고
    • RNA structure inhibits the TRAP (trp RNA-binding attenuation protein) -RNA interaction
    • Xirasager, S., M. B. Elliott, W. Bartolini, P. Gollnick, and P. Gottlieb. 1998. RNA structure inhibits the TRAP (trp RNA-binding attenuation protein) -RNA interaction. J. Biol. Chem. 273:27146-27153.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27146-27153
    • Xirasager, S.1    Elliott, M.B.2    Bartolini, W.3    Gollnick, P.4    Gottlieb, P.5
  • 38
    • 0037143667 scopus 로고    scopus 로고
    • NusA-stimulated RNA polymerase pausing and termination participates in the Bacillus subtilis trp operon attenuation mechanism in vitro
    • Yakhnin, A. V., and P. Babitzke, 2002. NusA-stimulated RNA polymerase pausing and termination participates in the Bacillus subtilis trp operon attenuation mechanism in vitro. Proc. Natl. Acad. Sci. USA 99:11067-11072.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11067-11072
    • Yakhnin, A.V.1    Babitzke, P.2
  • 39
    • 0034635443 scopus 로고    scopus 로고
    • Effects of mutations in the L-tryptophan binding pocket of the trp RNA-binding attenuation protein of Bacillus subtilis
    • Yakhnin, A. V., J. J. Trimble, C. R. Chiaro, and P. Babitzke. 2000. Effects of mutations in the L-tryptophan binding pocket of the trp RNA-binding attenuation protein of Bacillus subtilis. J. Biol. Chem. 275:4519-4524.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4519-4524
    • Yakhnin, A.V.1    Trimble, J.J.2    Chiaro, C.R.3    Babitzke, P.4
  • 40
    • 0034811041 scopus 로고    scopus 로고
    • Expression of the Bacillus subtilis trpEDCFBA operon is influenced by translational coupling and Rho termination factor
    • Yakhnin, H., J. E. Babiarz, A. V. Yakhnin, and P. Babitzke. 2001. Expression of the Bacillus subtilis trpEDCFBA operon is influenced by translational coupling and Rho termination factor. J. Bacteriol. 183:5918-5926.
    • (2001) J. Bacteriol. , vol.183 , pp. 5918-5926
    • Yakhnin, H.1    Babiarz, J.E.2    Yakhnin, A.V.3    Babitzke, P.4
  • 41
    • 0029120844 scopus 로고
    • Translation of trpG in Bacillus subtilis is regulated by the trp RNA-binding attenuation protein (TRAP)
    • Yang, M., A. de Saizieu, A. P. van Loon, and P. Golinick. 1995. Translation of trpG in Bacillus subtilis is regulated by the trp RNA-binding attenuation protein (TRAP). J. Bacteriol. 177:4272-4278.
    • (1995) J. Bacteriol. , vol.177 , pp. 4272-4278
    • Yang, M.1    De Saizieu, A.2    Van Loon, A.P.3    Golinick, P.4
  • 42
    • 0031214216 scopus 로고    scopus 로고
    • Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding
    • Yang, M., X.-P. Chen, and P. Gollnick. 1997. Alanine-scanning mutagenesis of Bacillus subtilis trp RNA-binding attenuation protein (TRAP) reveals residues involved in tryptophan binding and RNA binding. J. Mol. Biol. 270:696-710.
    • (1997) J. Mol. Biol. , vol.270 , pp. 696-710
    • Yang, M.1    Chen, X.-P.2    Gollnick, P.3
  • 43
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. 2003. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31:1-10.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1-10
    • Zuker, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.