메뉴 건너뛰기




Volumn 294, Issue 2, 1999, Pages 389-402

RNA recognition by transcriptional antiterminators of the BgIG/SacY family: Functional and structural comparison of the CAT domain from SacY and LicT

Author keywords

Antitermination; Bacillus subtilis; RNA binding; Surface plasmon resonance; X ray structure

Indexed keywords

AMINO ACID; DIMER; MESSENGER RNA; MONOMER; REGULATOR PROTEIN; RNA POLYMERASE;

EID: 0033607491     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3256     Document Type: Article
Times cited : (37)

References (34)
  • 1
    • 0026739805 scopus 로고
    • Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation
    • Amster-Choder O., Wright A. Modulation of the dimerization of a transcriptional antiterminator protein by phosphorylation. Science. 257:1992;1395-1398.
    • (1992) Science , vol.257 , pp. 1395-1398
    • Amster-Choder, O.1    Wright, A.2
  • 2
    • 0027339573 scopus 로고
    • Transcriptional regulation of the bgl operon of Escherichia coli involves phosphotransferase system-mediated phosphorylation of a transcriptional antiterminator
    • Amster-Choder O., Wright A. Transcriptional regulation of the bgl operon of Escherichia coli involves phosphotransferase system-mediated phosphorylation of a transcriptional antiterminator. J. Cell. Biochem. 51:1993;83-90.
    • (1993) J. Cell. Biochem. , vol.51 , pp. 83-90
    • Amster-Choder, O.1    Wright, A.2
  • 3
    • 0030931685 scopus 로고    scopus 로고
    • BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue
    • Amster-Choder O., Wright A. BglG, the response regulator of the Escherichia coli bgl operon, is phosphorylated on a histidine residue. J. Bacteriol. 179:1997;5621-5624.
    • (1997) J. Bacteriol. , vol.179 , pp. 5621-5624
    • Amster-Choder, O.1    Wright, A.2
  • 4
    • 0026772662 scopus 로고
    • Regulation of the sacPA operon of Bacillus subtilis: Identification of phosphotransferase system components involved in SacT activity
    • Arnaud M., Vary P., Zagorec M., Klier A., Débarbouillé M., Postma P., Rapoport G. Regulation of the sacPA operon of Bacillus subtilis: identification of phosphotransferase system components involved in SacT activity. J. Bacteriol. 174:1992;3161-3170.
    • (1992) J. Bacteriol. , vol.174 , pp. 3161-3170
    • Arnaud, M.1    Vary, P.2    Zagorec, M.3    Klier, A.4    Débarbouillé, M.5    Postma, P.6    Rapoport, G.7
  • 5
    • 0026465459 scopus 로고
    • Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family
    • Aymerich S., Steinmetz M. Specificity determinants and structural features in the RNA target of the bacterial antiterminator proteins of the BglG/SacY family. Proc. Natl Acad. Sci. USA. 89:1992;10410-10414.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10410-10414
    • Aymerich, S.1    Steinmetz, M.2
  • 6
    • 0031711025 scopus 로고    scopus 로고
    • Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system
    • Bachem S., Stulke J. Regulation of the Bacillus subtilis GlcT antiterminator protein by components of the phosphotransferase system. J. Bacteriol. 180:1998;5319-5326.
    • (1998) J. Bacteriol. , vol.180 , pp. 5319-5326
    • Bachem, S.1    Stulke, J.2
  • 9
    • 0025071240 scopus 로고
    • Solution structure of an unusually stable RNA hairpin, 5′GGAC(UUCG)GUCC
    • Cheong C., Varani G., Tinoco I. Jr. Solution structure of an unusually stable RNA hairpin, 5′GGAC(UUCG)GUCC. Nature. 346:1990;680-682.
    • (1990) Nature , vol.346 , pp. 680-682
    • Cheong, C.1    Varani, G.2    Tinoco I., Jr.3
  • 10
    • 0026669933 scopus 로고
    • Transcription of the Bacillus subtilis sacX and sacY genes, encoding regulators of sucrose metabolism, is both inducible by sucrose and controlled by the DegS-DegU signalling system
    • Crutz A. M., Steinmetz M. Transcription of the Bacillus subtilis sacX and sacY genes, encoding regulators of sucrose metabolism, is both inducible by sucrose and controlled by the DegS-DegU signalling system. J. Bacteriol. 174:1992;6087-6095.
    • (1992) J. Bacteriol. , vol.174 , pp. 6087-6095
    • Crutz, A.M.1    Steinmetz, M.2
  • 11
    • 0025301224 scopus 로고
    • The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators
    • Débarbouillé M., Arnaud M., Fouet A., Klier A., Rapoport G. The sacT gene regulating the sacPA operon in Bacillus subtilis shares strong homology with transcriptional antiterminators. J. Bacteriol. 172:1990;3966-3973.
    • (1990) J. Bacteriol. , vol.172 , pp. 3966-3973
    • Débarbouillé, M.1    Arnaud, M.2    Fouet, A.3    Klier, A.4    Rapoport, G.5
  • 12
    • 0025052636 scopus 로고
    • Transcriptional antitermination in the bgl operon of E. coli is modulated by a specific RNA binding protein
    • Houman F., Diaz-Torres M. R., Wright A. Transcriptional antitermination in the bgl operon of E. coli is modulated by a specific RNA binding protein. Cell. 62:1990;1153-1163.
    • (1990) Cell , vol.62 , pp. 1153-1163
    • Houman, F.1    Diaz-Torres, M.R.2    Wright, A.3
  • 13
    • 0031912636 scopus 로고    scopus 로고
    • SacY, a transcriptional antiterminator from Bacillus subtilis, is regulated by phosphorylation in vivo
    • Idelson M., Amster-Choder O. SacY, a transcriptional antiterminator from Bacillus subtilis, is regulated by phosphorylation in vivo. J. Bacteriol. 180:1998;660-666.
    • (1998) J. Bacteriol. , vol.180 , pp. 660-666
    • Idelson, M.1    Amster-Choder, O.2
  • 14
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski R. A., MacArtur M. W., Moss D. S., Thornton J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
    • (1993) J. Appl. Crystallog. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArtur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 15
    • 0028986940 scopus 로고
    • New beta-glucoside (bgl) genes in Bacillus subtilis: The bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog
    • Le Coq D., Lindner C., Kruger S., Steinmetz M., Stulke J. New beta-glucoside (bgl) genes in Bacillus subtilis: the bglP gene product has both transport and regulatory functions similar to those of BglF, its Escherichia coli homolog. J. Bacteriol. 177:1995;1527-1535.
    • (1995) J. Bacteriol. , vol.177 , pp. 1527-1535
    • Le, C.D.1    Lindner, C.2    Kruger, S.3    Steinmetz, M.4    Stulke, J.5
  • 17
    • 0030858903 scopus 로고    scopus 로고
    • Gene organisation and regulatory sequences in the sucrose utilisation cluster of Bacillus stearothermophilus NUB36
    • Li Y., Ferenci T. Gene organisation and regulatory sequences in the sucrose utilisation cluster of Bacillus stearothermophilus NUB36. Gene. 195:1997;195-200.
    • (1997) Gene , vol.195 , pp. 195-200
    • Li, Y.1    Ferenci, T.2
  • 18
    • 0032905438 scopus 로고    scopus 로고
    • Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- And HPr-catalysed phosphorylation
    • Lindner C., Galinier A., Hecker M., Deutscher J. Regulation of the activity of the Bacillus subtilis antiterminator LicT by multiple PEP-dependent, enzyme I- and HPr-catalysed phosphorylation. Mol. Microbiol. 31:1999;995-1006.
    • (1999) Mol. Microbiol. , vol.31 , pp. 995-1006
    • Lindner, C.1    Galinier, A.2    Hecker, M.3    Deutscher, J.4
  • 20
    • 0030746108 scopus 로고    scopus 로고
    • From genetic to structural characterization of a new class of RNA- binding domain within the SacY/BglG family of antiterminator proteins
    • Manival X., Yang Y., Strub M. P., Kochoyan M., Steinmetz M., Aymerich S. From genetic to structural characterization of a new class of RNA- binding domain within the SacY/BglG family of antiterminator proteins. EMBO J. 16:1997b;5019-5029.
    • (1997) EMBO J. , vol.16 , pp. 5019-5029
    • Manival, X.1    Yang, Y.2    Strub, M.P.3    Kochoyan, M.4    Steinmetz, M.5    Aymerich, S.6
  • 22
    • 84920325457 scopus 로고
    • AMoRe: An automated package of molecular replacement
    • Navaza J. AMoRe: an automated package of molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 23
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K. A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 26
    • 0029971285 scopus 로고    scopus 로고
    • LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family
    • Schnetz K., Stulke J., Gertz S., Kruger S., Krieg M., Hecker M., Rak B. LicT, a Bacillus subtilis transcriptional antiterminator protein of the BglG family. J. Bacteriol. 178:1996;1971-1979.
    • (1996) J. Bacteriol. , vol.178 , pp. 1971-1979
    • Schnetz, K.1    Stulke, J.2    Gertz, S.3    Kruger, S.4    Krieg, M.5    Hecker, M.6    Rak, B.7
  • 27
    • 0001954586 scopus 로고
    • Carbohydrate catabolism: Pathways, enzymes, genetic regulation and evolution
    • A. L. Sohenshein, J. A. Hoch, & R. Losick. Washington: American Society for Microbiology
    • Steinmetz M. Carbohydrate catabolism: pathways, enzymes, genetic regulation and evolution. Sohenshein A. L., Hoch J. A., Losick R. Bacillus subtilis, and other Gram-positive Bacteria, Biochemistry, Physiology, and Molecular Genetics. 1993;157-170 American Society for Microbiology, Washington.
    • (1993) Bacillus Subtilis, and Other Gram-positive Bacteria, Biochemistry, Physiology, and Molecular Genetics , pp. 157-170
    • Steinmetz, M.1
  • 28
    • 0031808469 scopus 로고    scopus 로고
    • PRD-a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria
    • Stulke J., Arnaud M., Rapoport G., Martin-Verstraete I. PRD-a protein domain involved in PTS-dependent induction and carbon catabolite repression of catabolic operons in bacteria. Mol. Microbiol. 28:1998;865-874.
    • (1998) Mol. Microbiol. , vol.28 , pp. 865-874
    • Stulke, J.1    Arnaud, M.2    Rapoport, G.3    Martin-Verstraete, I.4
  • 29
    • 0032521544 scopus 로고    scopus 로고
    • Adaptation of an enzyme to regulatory function: Structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase
    • Tomchick D. R., Turner R. J., Switzer R. L., Smith J. L. Adaptation of an enzyme to regulatory function: structure of Bacillus subtilis PyrR, a pyr RNA-binding attenuation protein and uracil phosphoribosyltransferase. Structure. 6:1998;337-350.
    • (1998) Structure , vol.6 , pp. 337-350
    • Tomchick, D.R.1    Turner, R.J.2    Switzer, R.L.3    Smith, J.L.4
  • 30
    • 0030758035 scopus 로고    scopus 로고
    • Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system
    • Tortosa P., Aymerich S., Lindner C., Saier M. H. Jr, Reizer J., Le Coq D. Multiple phosphorylation of SacY, a Bacillus subtilis transcriptional antiterminator negatively controlled by the phosphotransferase system. J. Biol. Chem. 272:1997;17230-17237.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17230-17237
    • Tortosa, P.1    Aymerich, S.2    Lindner, C.3    Saier M.H., Jr.4    Reizer, J.5    Le, C.D.6
  • 31
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegard K., Murray J. B., Stockley P. G., Stonehouse N. J., Liljas L. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature. 371:1994;623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegard, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 32
    • 0030832399 scopus 로고    scopus 로고
    • Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis
    • van Tilbeurgh H., Manival X., Aymerich S., Lhoste J. M., Dumas C., Kochoyan M. Crystal structure of a new RNA-binding domain from the antiterminator protein SacY of Bacillus subtilis. EMBO J. 16:1997;5030-5036.
    • (1997) EMBO J. , vol.16 , pp. 5030-5036
    • Van Tilbeurgh, H.1    Manival, X.2    Aymerich, S.3    Lhoste, J.M.4    Dumas, C.5    Kochoyan, M.6
  • 33
    • 0026724966 scopus 로고
    • A family of bacterial regulators homologous to Gal and Lac repressors
    • Weickert M. J., Adhya S. A family of bacterial regulators homologous to Gal and Lac repressors. J. Biol. Chem. 267:1992;15869-15874.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15869-15874
    • Weickert, M.J.1    Adhya, S.2
  • 34
    • 0029739903 scopus 로고    scopus 로고
    • Quantitation of putative activator-target affinities predicts transcriptional activating potentials
    • Wu Y., Reece R. J., Ptashne M. Quantitation of putative activator-target affinities predicts transcriptional activating potentials. EMBO J. 15:1996;3951-3963.
    • (1996) EMBO J. , vol.15 , pp. 3951-3963
    • Wu, Y.1    Reece, R.J.2    Ptashne, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.