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Volumn 10, Issue 9, 1996, Pages 1143-1151

The RNA-binding protein HF-I, known as a host factor for phage Qβ RNA replication, is essential for rpoS translation in Escherichia coli

Author keywords

mRNA secondary structure; osmotic regulation; stationary phase; factor; (s)

Indexed keywords

MESSENGER RNA; RNA BINDING PROTEIN;

EID: 0029897937     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.10.9.1143     Document Type: Article
Times cited : (224)

References (39)
  • 1
    • 0027282394 scopus 로고
    • Different mechanisms of recognition of bacteriophage Qβ plus and minus strand RNAs by Qβ replicase
    • Barrera, I., D. Schuppli, J.M. Sogo, and H. Weber. 1993. Different mechanisms of recognition of bacteriophage Qβ plus and minus strand RNAs by Qβ replicase. J. Mol. Biol. 232: 512-521.
    • (1993) J. Mol. Biol. , vol.232 , pp. 512-521
    • Barrera, I.1    Schuppli, D.2    Sogo, J.M.3    Weber, H.4
  • 3
    • 0017683069 scopus 로고
    • Host factor for coliphage Qσ RNA replication: Presence in prokaryotes and association with the 30S ribosomal subunit in Escherichia coli
    • DuBow, M., T. Ryan, R.A. Young, and T. Blumenthal. 1977. Host factor for coliphage Qσ RNA replication: Presence in prokaryotes and association with the 30S ribosomal subunit in Escherichia coli. Mol. & Gen. Genet. 153: 39-43.
    • (1977) Mol. & Gen. Genet. , vol.153 , pp. 39-43
    • DuBow, M.1    Ryan, T.2    Young, R.A.3    Blumenthal, T.4
  • 4
    • 0014409656 scopus 로고
    • Factor fraction required for the synthesis of bacteriophage Qβ RNA
    • Franze de Fernandez, M.T., L. Eoyang, and J.T. August. 1968. Factor fraction required for the synthesis of bacteriophage Qβ RNA. Nature 219: 588-590.
    • (1968) Nature , vol.219 , pp. 588-590
    • Franze De Fernandez, M.T.1    Eoyang, L.2    August, J.T.3
  • 5
    • 0015500282 scopus 로고
    • Bacterial proteins required for replication of phage Qβ ribonucleic acid. Purification and properties of host factor I, a ribonucleic acid-binding protein
    • Franze de Fernandez, M.T., W.S. Hayward, and J.T. August. 1972. Bacterial proteins required for replication of phage Qβ ribonucleic acid. Purification and properties of host factor I, a ribonucleic acid-binding protein. J. Biol. Chem. 247: 824-831.
    • (1972) J. Biol. Chem. , vol.247 , pp. 824-831
    • Franze De Fernandez, M.T.1    Hayward, W.S.2    August, J.T.3
  • 7
    • 0027509821 scopus 로고
    • Survival of hunger and stress: The role of rpoS in stationary phase gene regulation in Escherichia coli
    • Hengge-Aronis, R. 1993. Survival of hunger and stress: The role of rpoS in stationary phase gene regulation in Escherichia coli. Cell 72: 165-168.
    • (1993) Cell , vol.72 , pp. 165-168
    • Hengge-Aronis, R.1
  • 8
    • 0023833060 scopus 로고
    • A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli
    • Higgins, C.F., C.J. Dorman, D.A. Stirling, L. Waddell, I.R. Booth, G. May, and E. Bremer. 1988. A physiological role for DNA supercoiling in the osmotic regulation of gene expression in S. typhimurium and E. coli. Cell 52: 569-584.
    • (1988) Cell , vol.52 , pp. 569-584
    • Higgins, C.F.1    Dorman, C.J.2    Stirling, D.A.3    Waddell, L.4    Booth, I.R.5    May, G.6    Bremer, E.7
  • 9
    • 0026067069 scopus 로고
    • Identification and sequence determination of the host factor gene for bacteriophage Qβ
    • Kajitani, M. and A. Ishihama. 1991. Identification and sequence determination of the host factor gene for bacteriophage Qβ. Nucleic Acids Res. 19: 1063-1066.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1063-1066
    • Kajitani, M.1    Ishihama, A.2
  • 10
    • 0014936343 scopus 로고
    • Characterization of the subunits of Qβ replicase
    • Kamen, R. 1970. Characterization of the subunits of Qβ replicase. Nature 228: 527-533.
    • (1970) Nature , vol.228 , pp. 527-533
    • Kamen, R.1
  • 11
    • 0028246273 scopus 로고
    • The expression of nifA in Azorhizobium caulinodans requires a gene product homologous to Escherichia coli HF-I, an RNA-binding protein involved in the replication of phage Qβ RNA
    • Kaminski, P.A., N. Desnoues, and C Elmerich. 1994. The expression of nifA in Azorhizobium caulinodans requires a gene product homologous to Escherichia coli HF-I, an RNA-binding protein involved in the replication of phage Qβ RNA. Proc. Natl. Acad. Sci. 91: 4663-4667.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 4663-4667
    • Kaminski, P.A.1    Desnoues, N.2    Elmerich, C.3
  • 12
    • 0014936354 scopus 로고
    • Subunit structure of Qβ replicase
    • Kondo, M., R. Gallerani, and C. Weissmann. 1970. Subunit structure of Qβ replicase. Nature 228: 525-527.
    • (1970) Nature , vol.228 , pp. 525-527
    • Kondo, M.1    Gallerani, R.2    Weissmann, C.3
  • 14
    • 0026020230 scopus 로고
    • Identification of a central regulator of stationaryphase gene expression in Escherichia coli
    • _. 1991b. Identification of a central regulator of stationaryphase gene expression in Escherichia coli. Mol. Microbiol. 5: 49-59.
    • (1991) Mol. Microbiol. , vol.5 , pp. 49-59
  • 15
    • 0028176450 scopus 로고
    • S subunit of RNA-polymerase in Escherichia coli is controlled at the levels of transcription, translation and protein stability
    • S subunit of RNA-polymerase in Escherichia coli is controlled at the levels of transcription, translation and protein stability. Genes & Dev. 8: 1600-1612.
    • (1994) Genes & Dev. , vol.8 , pp. 1600-1612
  • 16
    • 0028106775 scopus 로고
    • The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation
    • _. 1994b. The nlpD gene is located in an operon with rpoS on the Escherichia coli chromosome and encodes a novel lipoprotein with a potential function in cell wall formation. Mol. Microbiol. 13: 733-743.
    • (1994) Mol. Microbiol. , vol.13 , pp. 733-743
  • 20
    • 0028289538 scopus 로고
    • Adaptation of Escherichia coli to high osmolarity environments: Osmoregulation of the high-affinity glycine betaine transport system ProU
    • Lucht, J.M. and E. Bremer. 1994. Adaptation of Escherichia coli to high osmolarity environments: Osmoregulation of the high-affinity glycine betaine transport system ProU. FEMS Microbiol. Rev. 14: 3-20.
    • (1994) FEMS Microbiol. Rev. , vol.14 , pp. 3-20
    • Lucht, J.M.1    Bremer, E.2
  • 21
    • 0025785253 scopus 로고
    • The putative σ factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli
    • McCann, M.P., J.P. Kidwell, and A. Matin. 1991. The putative σ factor KatF has a central role in development of starvation-mediated general resistance in Escherichia coli. J. Bacteriol. 173:4188-4194.
    • (1991) J. Bacteriol. , vol.173 , pp. 4188-4194
    • McCann, M.P.1    Kidwell, J.P.2    Matin, A.3
  • 22
    • 0027412046 scopus 로고
    • The putative σ factor KatF is regulated posttranscriptionally during carbon starvation
    • McCann, M.P., C.D. Fraley, and A. Matin. 1993. The putative σ factor KatF is regulated posttranscriptionally during carbon starvation. J. Bacteriol. 175: 2143-2149.
    • (1993) J. Bacteriol. , vol.175 , pp. 2143-2149
    • McCann, M.P.1    Fraley, C.D.2    Matin, A.3
  • 26
    • 0025788228 scopus 로고
    • 32 synthesis during the heat shock response of Escherichia coli
    • 32 synthesis during the heat shock response of Escherichia coli. Proc. Natl. Acad. Sci. 88: 10515-10519.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 10515-10519
    • Nagai, H.1    Yuzawa, H.2    Yura, T.3
  • 27
    • 0026754366 scopus 로고
    • The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression
    • Owen-Hughes, T.A., G.D. Pavitt, D.S. Santos, J.M. Sidebotham, C.S. Hulton, J.C.D. Hinton, and C.F. Higgins. 1992. The chromatin-associated protein H-NS interacts with curved DNA to influence DNA topology and gene expression. Cell 71: 255-265.
    • (1992) Cell , vol.71 , pp. 255-265
    • Owen-Hughes, T.A.1    Pavitt, G.D.2    Santos, D.S.3    Sidebotham, J.M.4    Hulton, C.S.5    Hinton, J.C.D.6    Higgins, C.F.7
  • 29
    • 0017227834 scopus 로고
    • Site-specific interaction of Qβ host factor and ribosomal protein Sl with Qβ and R17 bacteriophage RNAs
    • Senear, A.W. and J.A. Steitz. 1976. Site-specific interaction of Qβ host factor and ribosomal protein Sl with Qβ and R17 bacteriophage RNAs. J. Biol. Chem. 251: 1902-1912.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1902-1912
    • Senear, A.W.1    Steitz, J.A.2
  • 31
    • 0021760528 scopus 로고
    • H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro
    • Spassky, A., S. Rimsky, H. Garreau, and H. Buc. 1984. H1a, an E. coli DNA-binding protein which accumulates in stationary phase, strongly compacts DNA in vitro. Nucleic Acids Res. 12: 5321-5340.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5321-5340
    • Spassky, A.1    Rimsky, S.2    Garreau, H.3    Buc, H.4
  • 32
    • 0028567464 scopus 로고
    • Regulation of translation by specific protein/mRNA interactions
    • Standart, N. and R.J. Jackson. 1994. Regulation of translation by specific protein/mRNA interactions. Biochimie 76: 867-879.
    • (1994) Biochimie , vol.76 , pp. 867-879
    • Standart, N.1    Jackson, R.J.2
  • 33
    • 0028362445 scopus 로고
    • Structure of the 5′ upstream region and the regulation of the rpoS gene of Escherichia coli
    • Takayanagi, Y., K. Tanaka, and H. Takahashi. 1994. Structure of the 5′ upstream region and the regulation of the rpoS gene of Escherichia coli. Mol. &. Gen. Genet. 243: 525-531.
    • (1994) Mol. &. Gen. Genet. , vol.243 , pp. 525-531
    • Takayanagi, Y.1    Tanaka, K.2    Takahashi, H.3
  • 35
    • 0028243445 scopus 로고
    • Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12
    • Tsui, H.-C.T., H.-C.L. Leung, and M.E. Winkler. 1994. Characterization of broadly pleiotropic phenotypes caused by an hfq insertion mutation in Escherichia coli K-12. mol. Microbiol. 13: 35-49.
    • (1994) Mol. Microbiol. , vol.13 , pp. 35-49
    • Tsui, H.-C.T.1    Leung, H.-C.L.2    Winkler, M.E.3
  • 37
    • 0028895391 scopus 로고
    • S, in Escherichia coli: Involvement of the nucleoid protein H-NS
    • S, in Escherichia coli: Involvement of the nucleoid protein H-NS. EMBO J. 14: 594-602.
    • (1995) EMBO J. , vol.14 , pp. 594-602
    • Yamashino, T.1    Ueguchi, C.2    Mizuno, T.3
  • 38
    • 0027385183 scopus 로고
    • Regulation of the heat-shock response in bacteria
    • Yura, T., H. Nagai, and H. Mori. 1993. Regulation of the heat-shock response in bacteria. Annu. Rev. Microbiol. 47: 321-350.
    • (1993) Annu. Rev. Microbiol. , vol.47 , pp. 321-350
    • Yura, T.1    Nagai, H.2    Mori, H.3
  • 39
    • 0027521148 scopus 로고
    • 32 synthesis mediated by mRNA secondary structure: A primary step of the heat shock response in Escherichia coli
    • 32 synthesis mediated by mRNA secondary structure: A primary step of the heat shock response in Escherichia coli. Nucleic Acids Res. 21: 5449-5455.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5449-5455
    • Yuzawa, H.1    Nagai, H.2    Mon, H.3    Yura, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.