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Volumn 50, Issue 5, 2003, Pages 1605-1615

Ssh10b, a conserved thermophilic archaeal protein, binds RNA in vivo

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; DOUBLE STRANDED DNA; MESSENGER RNA; RIBOSOME RNA; RNA; RNA 16S; RNA 23S; SAC10B PROTEIN; SINGLE STRANDED DNA; SINGLE STRANDED RNA; SSH10B PROTEIN; UNCLASSIFIED DRUG;

EID: 0346256792     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2003.03793.x     Document Type: Article
Times cited : (66)

References (42)
  • 1
    • 0032977614 scopus 로고    scopus 로고
    • Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2
    • Afshar, G., and Murnane, J.P. (1999) Characterization of a human gene with sequence homology to Saccharomyces cerevisiae SIR2. Gene 234: 161-168.
    • (1999) Gene , vol.234 , pp. 161-168
    • Afshar, G.1    Murnane, J.P.2
  • 2
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam, T., Iwata, A., Nishimura, A., Ueda, S., and Ishihama, A. (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J Bacteriol 181: 6361-6370.
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 3
    • 0033869982 scopus 로고    scopus 로고
    • Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid
    • Azam, T.A., Hiraga, S., and Ishihama, A. (2000) Two types of localization of the DNA-binding proteins within the Escherichia coli nucleoid. Genes Cells 5: 613-626.
    • (2000) Genes Cells , vol.5 , pp. 613-626
    • Azam, T.A.1    Hiraga, S.2    Ishihama, A.3
  • 4
    • 0035117825 scopus 로고    scopus 로고
    • The Escherichia coli histone-like protein HU regulates rpoS translation
    • Balandina, A., Claret, L., Hengge-Aronis, R., and Rouviere-Yaniv, J. (2001) The Escherichia coli histone-like protein HU regulates rpoS translation. Mol Microbiol 39: 1069-1079.
    • (2001) Mol Microbiol , vol.39 , pp. 1069-1079
    • Balandina, A.1    Claret, L.2    Hengge-Aronis, R.3    Rouviere-Yaniv, J.4
  • 5
    • 0037008678 scopus 로고    scopus 로고
    • The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids
    • Balandina, A., Kamashev, D., and Rouviere-Yaniv, J. (2002) The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids. J Biol Chem 277: 27622-27628.
    • (2002) J Biol Chem , vol.277 , pp. 27622-27628
    • Balandina, A.1    Kamashev, D.2    Rouviere-Yaniv, J.3
  • 6
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Baumann, H., Knapp, S., Lundback, T., Ladenstein, R., and Hard, T. (1994) Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat Struct Biol 1: 808-819.
    • (1994) Nat Struct Biol , vol.1 , pp. 808-819
    • Baumann, H.1    Knapp, S.2    Lundback, T.3    Ladenstein, R.4    Hard, T.5
  • 7
    • 0037023326 scopus 로고    scopus 로고
    • The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation
    • Bell, S.D., Botting, C.H., Wardleworth, B.N., Jackson, S.P., and White, M.F. (2002) The interaction of Alba, a conserved archaeal chromatin protein, with Sir2 and its regulation by acetylation. Science 296: 148-151.
    • (2002) Science , vol.296 , pp. 148-151
    • Bell, S.D.1    Botting, C.H.2    Wardleworth, B.N.3    Jackson, S.P.4    White, M.F.5
  • 9
    • 0028136642 scopus 로고
    • DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA
    • Bonnefoy, E., Takahashi, M., and Yaniv, J.R. (1994) DNA-binding parameters of the HU protein of Escherichia coli to cruciform DNA. J Mol Biol 242: 116-129.
    • (1994) J Mol Biol , vol.242 , pp. 116-129
    • Bonnefoy, E.1    Takahashi, M.2    Yaniv, J.R.3
  • 10
    • 0015275944 scopus 로고
    • Sulfolobus: A new genus of sulfur-oxidizing bacteria living at low pH and high temperature
    • Brock, T.D., Brock, K.M., Belly, R.T., and Weiss, R.L. (1972) Sulfolobus: a new genus of sulfur-oxidizing bacteria living at low pH and high temperature. Arch Mikrobiol 84: 54-68.
    • (1972) Arch Mikrobiol , vol.84 , pp. 54-68
    • Brock, T.D.1    Brock, K.M.2    Belly, R.T.3    Weiss, R.L.4
  • 11
    • 0028901705 scopus 로고
    • HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps
    • Castaing, B., Zelwer, C., Laval, J., and Boiteux, S. (1995) HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps. J Biol Chem 270: 10291-10296.
    • (1995) J Biol Chem , vol.270 , pp. 10291-10296
    • Castaing, B.1    Zelwer, C.2    Laval, J.3    Boiteux, S.4
  • 12
    • 0347322186 scopus 로고    scopus 로고
    • Evolutionary conservation and DNA binding properties of the Ssh7 proteins from Sulfolobus shibatae
    • Chen, X., Guo, R., and Huang, L. (2002) Evolutionary conservation and DNA binding properties of the Ssh7 proteins from Sulfolobus shibatae. Sci China (Series C) 45: 583-592.
    • (2002) Sci China (Series C) , vol.45 , pp. 583-592
    • Chen, X.1    Guo, R.2    Huang, L.3
  • 13
    • 0037478787 scopus 로고    scopus 로고
    • Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms
    • Chou, C.C., Lin, T.W., Chen, C.Y., and Wang, A.H. (2003) Crystal structure of the hyperthermophilic archaeal DNA-binding protein Sso10b2 at a resolution of 1.85 Angstroms. J Bacteriol 185: 4066-4073.
    • (2003) J Bacteriol , vol.185 , pp. 4066-4073
    • Chou, C.C.1    Lin, T.W.2    Chen, C.Y.3    Wang, A.H.4
  • 14
    • 0034759978 scopus 로고    scopus 로고
    • Interaction of translation initiation factor 3 with the 30S ribosomal subunit
    • Dallas, A., and Noller, H.F. (2001) Interaction of translation initiation factor 3 with the 30S ribosomal subunit. Mol Cell 8: 855-864.
    • (2001) Mol Cell , vol.8 , pp. 855-864
    • Dallas, A.1    Noller, H.F.2
  • 15
    • 0003082897 scopus 로고
    • The structure of DNA-binding proteins from eu- and archaebacteria
    • Gualerzi, C.O., and Pon, C.L. (eds). New York: Springer-Verlag
    • Dijk, J., and Reinhardt, R. (1986) The structure of DNA-binding proteins from eu-and archaebacteria. In: Bacterial Chromatin. Gualerzi, C.O., and Pon, C.L. (eds). New York: Springer-Verlag, pp. 185-218.
    • (1986) Bacterial Chromatin , pp. 185-218
    • Dijk, J.1    Reinhardt, R.2
  • 16
    • 0023413620 scopus 로고
    • Histone-like proteins of bacteria
    • Drlica, K., and Rouviere-Yaniv, J. (1987) Histone-like proteins of bacteria. Microbiol Rev 51: 301-319.
    • (1987) Microbiol Rev , vol.51 , pp. 301-319
    • Drlica, K.1    Rouviere-Yaniv, J.2
  • 17
    • 0014596585 scopus 로고
    • Nucleotide sequences from specific areas of the 16S and 23S ribosomal RNAs of E. coli
    • Fellner, P. (1969) Nucleotide sequences from specific areas of the 16S and 23S ribosomal RNAs of E. coli. Eur J Biochem 11: 12-27.
    • (1969) Eur J Biochem , vol.11 , pp. 12-27
    • Fellner, P.1
  • 18
    • 0032961053 scopus 로고    scopus 로고
    • Identification of the gene encoding archaeal-specific DNA-binding proteins of the Sac10b family
    • Forterre, P., Confalonieri, F., and Knapp, S. (1999) Identification of the gene encoding archaeal-specific DNA-binding proteins of the Sac10b family. Mol Microbiol 32: 669-670.
    • (1999) Mol Microbiol , vol.32 , pp. 669-670
    • Forterre, P.1    Confalonieri, F.2    Knapp, S.3
  • 19
    • 0022478821 scopus 로고
    • Ribosomal and DNA binding proteins of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius
    • Grote, M., Dijk, J., and Reinhardt, R. (1986) Ribosomal and DNA binding proteins of the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. Biochim Biophys Acta 873: 405-413.
    • (1986) Biochim Biophys Acta , vol.873 , pp. 405-413
    • Grote, M.1    Dijk, J.2    Reinhardt, R.3
  • 20
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • Gualerzi, C.O., and Pon, C.L. (1990) Initiation of mRNA translation in prokaryotes. Biochemistry 29: 5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 21
    • 0034677535 scopus 로고    scopus 로고
    • Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase
    • Imai, S., Armstrong, C.M., Kaeberlein, M., and Guarente, L. (2000) Transcriptional silencing and longevity protein Sir2 is an NAD-dependent histone deacetylase. Nature 403: 795-800.
    • (2000) Nature , vol.403 , pp. 795-800
    • Imai, S.1    Armstrong, C.M.2    Kaeberlein, M.3    Guarente, L.4
  • 22
    • 0033214062 scopus 로고    scopus 로고
    • The binding motif recognized by HU on both nicked and cruciform DNA
    • Kamashev, D., Balandina, A., and Rouviere-Yaniv, J. (1999) The binding motif recognized by HU on both nicked and cruciform DNA. EMBO J 18: 5434-5444.
    • (1999) EMBO J , vol.18 , pp. 5434-5444
    • Kamashev, D.1    Balandina, A.2    Rouviere-Yaniv, J.3
  • 23
    • 0025820457 scopus 로고
    • Growth rate regulation of translation initiation factor IF3 biosynthesis in Escherichia coli
    • Liveris, D., Klotsky, R.A., and Schwartz, I. (1991) Growth rate regulation of translation initiation factor IF3 biosynthesis in Escherichia coli. J Bacteriol 173: 3888-3893.
    • (1991) J Bacteriol , vol.173 , pp. 3888-3893
    • Liveris, D.1    Klotsky, R.A.2    Schwartz, I.3
  • 24
    • 0022619406 scopus 로고
    • Total reconstitution of active large ribosomal subunits of the thermoacidophilic archaebacterium Sulfolobus solfataricus
    • Londei, P., Teixido, J., Acca, M., Cammarano, P., and Amils, R. (1986) Total reconstitution of active large ribosomal subunits of the thermoacidophilic archaebacterium Sulfolobus solfataricus. Nucleic Acids Res 14: 2269-2285.
    • (1986) Nucleic Acids Res , vol.14 , pp. 2269-2285
    • Londei, P.1    Teixido, J.2    Acca, M.3    Cammarano, P.4    Amils, R.5
  • 25
    • 2642690670 scopus 로고    scopus 로고
    • In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth
    • Lopez-Garcia, P., Knapp, S., Ladenstein, R., and Forterre, P. (1998) In vitro DNA binding of the archaeal protein Sso7d induces negative supercoiling at temperatures typical for thermophilic growth. Nucleic Acids Res 26: 2322-2328.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2322-2328
    • Lopez-Garcia, P.1    Knapp, S.2    Ladenstein, R.3    Forterre, P.4
  • 26
    • 0031957673 scopus 로고    scopus 로고
    • Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils
    • Mai, V.Q., Chen, X., Hong, R., and Huang, L. (1998) Small abundant DNA binding proteins from the thermoacidophilic archaeon Sulfolobus shibatae constrain negative DNA supercoils. J Bacteriol 180: 2560-2563.
    • (1998) J Bacteriol , vol.180 , pp. 2560-2563
    • Mai, V.Q.1    Chen, X.2    Hong, R.3    Huang, L.4
  • 27
    • 0029156641 scopus 로고
    • Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius
    • McAfee, J.G., Edmondson, S.P., Datta, P.K., Shriver, J.W., and Gupta, R. (1995) Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius. Biochemistry 34: 10063-10077.
    • (1995) Biochemistry , vol.34 , pp. 10063-10077
    • McAfee, J.G.1    Edmondson, S.P.2    Datta, P.K.3    Shriver, J.W.4    Gupta, R.5
  • 28
    • 0035881527 scopus 로고    scopus 로고
    • Translation initiation factor IF3: Two domains, five functions, one mechanism?
    • Petrelli, D., LaTeana, A., Garofalo, C., Spurio, R., Pon, C.L., and Gualerzi, C.O. (2001) Translation initiation factor IF3: two domains, five functions, one mechanism? EMBO J 20: 4560-4569.
    • (2001) EMBO J , vol.20 , pp. 4560-4569
    • Petrelli, D.1    LaTeana, A.2    Garofalo, C.3    Spurio, R.4    Pon, C.L.5    Gualerzi, C.O.6
  • 29
    • 0033515646 scopus 로고    scopus 로고
    • Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA
    • Pinson, V., Takahashi, M., and Rouviere-Yaniv, J. (1999) Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA. J Mol Biol 287: 485-497.
    • (1999) J Mol Biol , vol.287 , pp. 485-497
    • Pinson, V.1    Takahashi, M.2    Rouviere-Yaniv, J.3
  • 31
    • 0032426951 scopus 로고    scopus 로고
    • Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome
    • Sandman, K., Pereira, S.L., and Reeve, J.N. (1998) Diversity of prokaryotic chromosomal proteins and the origin of the nucleosome. Cell Mol Life Sci 54: 1350-1364.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 1350-1364
    • Sandman, K.1    Pereira, S.L.2    Reeve, J.N.3
  • 34
    • 0018081142 scopus 로고
    • Specific association of two homologous DNA-binding proteins to the native 30-S ribosomal subunits of Escherichia coli
    • Suryanarayana, T., and Subramanian, A.R. (1978) Specific association of two homologous DNA-binding proteins to the native 30-S ribosomal subunits of Escherichia coli. Biochim Biophys Acta 520: 342-357.
    • (1978) Biochim Biophys Acta , vol.520 , pp. 342-357
    • Suryanarayana, T.1    Subramanian, A.R.2
  • 35
    • 0029745401 scopus 로고    scopus 로고
    • Escherichia coli translation initiation factor 3 discriminates the initiation codon in vivo
    • Sussman, J.K., Simons, E.L., and Simons, R.W. (1996) Escherichia coli translation initiation factor 3 discriminates the initiation codon in vivo. Mol Microbiol 21: 347-360.
    • (1996) Mol Microbiol , vol.21 , pp. 347-360
    • Sussman, J.K.1    Simons, E.L.2    Simons, R.W.3
  • 36
    • 0041312645 scopus 로고    scopus 로고
    • Flexible DNA bending in HU-DNA cocrystal structures
    • Swinger, K.K., Lemberg, K.M., Zhang, Y., and Rice, P.A. (2003) Flexible DNA bending in HU-DNA cocrystal structures. EMBO J 22: 3749-3760.
    • (2003) EMBO J , vol.22 , pp. 3749-3760
    • Swinger, K.K.1    Lemberg, K.M.2    Zhang, Y.3    Rice, P.A.4
  • 37
    • 0021286693 scopus 로고
    • 3-A resolution structure of a protein with histone-like properties in prokaryotes
    • Tanaka, I., Appelt, K., Dijk, J., White, S.W., and Wilson, K.S. (1984) 3-A resolution structure of a protein with histone-like properties in prokaryotes. Nature 310: 376-381.
    • (1984) Nature , vol.310 , pp. 376-381
    • Tanaka, I.1    Appelt, K.2    Dijk, J.3    White, S.W.4    Wilson, K.S.5
  • 38
    • 0032896616 scopus 로고    scopus 로고
    • Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs
    • Tedin, K., Moll, I., Grill, S., Resch, A., Graschopf, A., Gualerzi, C.O., and Blasi, U. (1999) Translation initiation factor 3 antagonizes authentic start codon selection on leaderless mRNAs. Mol Microbiol 31: 67-77.
    • (1999) Mol Microbiol , vol.31 , pp. 67-77
    • Tedin, K.1    Moll, I.2    Grill, S.3    Resch, A.4    Graschopf, A.5    Gualerzi, C.O.6    Blasi, U.7
  • 39
    • 0037009516 scopus 로고    scopus 로고
    • Structure of Alba: An archaeal chromatin protein modulated by acetylation
    • Wardleworth, B.N., Russell, R.J., Bell, S.D., Taylor, G.L., and White, M.F. (2002) Structure of Alba: an archaeal chromatin protein modulated by acetylation. EMBO J 21: 4654-4662.
    • (2002) EMBO J , vol.21 , pp. 4654-4662
    • Wardleworth, B.N.1    Russell, R.J.2    Bell, S.D.3    Taylor, G.L.4    White, M.F.5
  • 40
    • 0033917479 scopus 로고    scopus 로고
    • An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion
    • Xue, H., Guo, R., Wen, Y., Liu, D., and Huang, L. (2000) An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. J Bacteriol 182: 3929-3933.
    • (2000) J Bacteriol , vol.182 , pp. 3929-3933
    • Xue, H.1    Guo, R.2    Wen, Y.3    Liu, D.4    Huang, L.5
  • 41
    • 0032720484 scopus 로고    scopus 로고
    • Cloning of a Leishmania major gene encoding for an antigen with extensive homology to ribosomal protein S3a
    • Zemzoumi, K., Guilvard, E., Sereno, D., Preto, A., Benlemlih, M., and Da Silva, A.C. (1999) Cloning of a Leishmania major gene encoding for an antigen with extensive homology to ribosomal protein S3a. Gene 240: 57-65.
    • (1999) Gene , vol.240 , pp. 57-65
    • Zemzoumi, K.1    Guilvard, E.2    Sereno, D.3    Preto, A.4    Benlemlih, M.5    Da Silva, A.C.6
  • 42
    • 0038168161 scopus 로고    scopus 로고
    • Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA binding
    • Zhao, K., Chai, X., and Marmorstein, R. (2003) Structure of a Sir2 substrate, Alba, reveals a mechanism for deacetylation-induced enhancement of DNA binding. J Biol Chem 278: 26071-26077.
    • (2003) J Biol Chem , vol.278 , pp. 26071-26077
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


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