메뉴 건너뛰기




Volumn 136, Issue 5, 2004, Pages 693-699

Kinetic analysis of precursor M1 RNA molecules for exploring substrate specificity of the N-terminal catalytic half of RNase E

Author keywords

Kinetic parameters; M1 RNA; RNase E; rne dependent site; Substrate specificity

Indexed keywords

RIBONUCLEASE; RIBONUCLEASE E; RNA; RNA PRECURSOR; UNCLASSIFIED DRUG;

EID: 14944375100     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh176     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0018034154 scopus 로고
    • Structural analysis and in vitro processing to p5S rRNA of a 9S RNA molecule isolated from an rne mutant of E. coli
    • Ghora, B.K. and Apirion, D. (1978) Structural analysis and in vitro processing to p5S rRNA of a 9S RNA molecule isolated from an rne mutant of E. coli. Cell 15, 1055-1066
    • (1978) Cell , vol.15 , pp. 1055-1066
    • Ghora, B.K.1    Apirion, D.2
  • 2
    • 0026447906 scopus 로고
    • Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein
    • Casaregola, S., Jacq, A., Laoudj, D., McGurk, G., Margarson, S., Tempete, M., Norris, V., and Holland, I.B. (1992) Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein. J. Mol. Biol. 228, 30-40
    • (1992) J. Mol. Biol. , vol.228 , pp. 30-40
    • Casaregola, S.1    Jacq, A.2    Laoudj, D.3    McGurk, G.4    Margarson, S.5    Tempete, M.6    Norris, V.7    Holland, I.B.8
  • 3
    • 43949161496 scopus 로고
    • Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein
    • Casaregola, S., Jacq, A., Laoudj, D., McGurk, G., Margarson, S., Tempete, M., Norris, V, and Holland, I.B. (1994) Cloning and analysis of the entire Escherichia coli ams gene, ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein. J. Mol. Biol. 238, 867
    • (1994) J. Mol. Biol. , vol.238 , pp. 867
    • Casaregola, S.1    Jacq, A.2    Laoudj, D.3    McGurk, G.4    Margarson, S.5    Tempete, M.6    Norris, V.7    Holland, I.B.8
  • 4
    • 0018582283 scopus 로고
    • RNase E, an RNA processing enzyme from Escherichia coli
    • Misra, T.K. and Apirion, D. (1979) RNase E, an RNA processing enzyme from Escherichia coli. J. Biol. Chem. 254, 11154-11159
    • (1979) J. Biol. Chem. , vol.254 , pp. 11154-11159
    • Misra, T.K.1    Apirion, D.2
  • 5
    • 0026008229 scopus 로고    scopus 로고
    • The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli
    • Babitzke, P. and Kushner, S.R. (1996) The Ams (altered mRNA stability) protein and ribonuclease E are encoded by the same structural gene of Escherichia coli. Proc. Natl Acad. Sci. USA 88, 1-5
    • (1996) Proc. Natl Acad. Sci. USA , vol.88 , pp. 1-5
    • Babitzke, P.1    Kushner, S.R.2
  • 6
    • 0025906534 scopus 로고
    • Genetic studies of cleavage-initiated mRNA decay and processing of ribosomal 9S RNA show that the Escherichia coli ams and rne loci are the same
    • Melefors, O. and von Gabain, A. (1991) Genetic studies of cleavage-initiated mRNA decay and processing of ribosomal 9S RNA show that the Escherichia coli ams and rne loci are the same. Mol. Microbiol. 5, 857-864
    • (1991) Mol. Microbiol. , vol.5 , pp. 857-864
    • Melefors, O.1    Von Gabain, A.2
  • 7
    • 0025688893 scopus 로고
    • RNase E, an endoribonuclease, has a general role in the chemical decay of Escherichia coli mRNA: Evidence that rne and ams are the same genetic locus
    • Mudd, E.A., Krisch, H.M., and Higgins, C.F. (1990) RNase E, an endoribonuclease, has a general role in the chemical decay of Escherichia coli mRNA: evidence that rne and ams are the same genetic locus. Mol. Microbiol. 4, 2127-2135
    • (1990) Mol. Microbiol. , vol.4 , pp. 2127-2135
    • Mudd, E.A.1    Krisch, H.M.2    Higgins, C.F.3
  • 8
    • 0025881986 scopus 로고
    • The gene specifying RNase E (rne) and a gene affecting mRNA stability (ams) are the same gene
    • Taraseviciene, L., Miczak, A., and Apirion, D. (1991) The gene specifying RNase E (rne) and a gene affecting mRNA stability (ams) are the same gene. Mol. Microbiol. 5, 851-855
    • (1991) Mol. Microbiol. , vol.5 , pp. 851-855
    • Taraseviciene, L.1    Miczak, A.2    Apirion, D.3
  • 9
    • 0029962989 scopus 로고    scopus 로고
    • The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site
    • McDowall, K.J. and Cohen, S.N. (1996) The N-terminal domain of the rne gene product has RNase E activity and is non-overlapping with the arginine-rich RNA-binding site. J. Mol. Biol. 255, 349-355
    • (1996) J. Mol. Biol. , vol.255 , pp. 349-355
    • McDowall, K.J.1    Cohen, S.N.2
  • 10
    • 0027273009 scopus 로고
    • The ams-1 and rne-3071 temperature-sensitive mutations in the ams gene are in close proximity to each other and cause substitutions within a domain that resembles a product of the Escherichia coli mre locus
    • McDowall, K.J., Hernandez, R.G., Lin-Chao, S., and Cohen, S.N. (1993) The ams-1 and rne-3071 temperature-sensitive mutations in the ams gene are in close proximity to each other and cause substitutions within a domain that resembles a product of the Escherichia coli mre locus. J. Bacteriol. 175, 4245-4249
    • (1993) J. Bacteriol. , vol.175 , pp. 4245-4249
    • McDowall, K.J.1    Hernandez, R.G.2    Lin-Chao, S.3    Cohen, S.N.4
  • 11
    • 0028840292 scopus 로고
    • Evidence for an RNA binding region in the Escherichia coli processing endoribonuclease RNase E
    • Taraseviciene, L., Bjork, G.R., and Uhlin, B.E. (1995) Evidence for an RNA binding region in the Escherichia coli processing endoribonuclease RNase E. J. Biol. Chem. 270, 26391-26398
    • (1995) J. Biol. Chem. , vol.270 , pp. 26391-26398
    • Taraseviciene, L.1    Bjork, G.R.2    Uhlin, B.E.3
  • 12
    • 0032578486 scopus 로고    scopus 로고
    • The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly
    • Kaberdin, V.R., Miczak, A., Jakobsen, J.S., Lin-Chao, S., McDowall, K.J., and von Gabain, A. (1998) The endoribonucleolytic N-terminal half of Escherichia coli RNase E is evolutionarily conserved in Synechocystis sp. and other bacteria but not the C-terminal half, which is sufficient for degradosome assembly. Proc. Natl Acad. Sci. USA 95, 11637-11642
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 11637-11642
    • Kaberdin, V.R.1    Miczak, A.2    Jakobsen, J.S.3    Lin-Chao, S.4    McDowall, K.J.5    Von Gabain, A.6
  • 14
    • 0033214259 scopus 로고    scopus 로고
    • Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEAD-box RNA helicase
    • Coburn, G.A. and Mackie, G.A. (1999) Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3′ exonuclease and a DEAD-box RNA helicase. Genes Dev. 13, 2594-2603
    • (1999) Genes Dev. , vol.13 , pp. 2594-2603
    • Coburn, G.A.1    Mackie, G.A.2
  • 15
    • 0026559344 scopus 로고
    • Specificity of Escherichia coli endoribonuclease RNase E: In vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site
    • Ehretsmann, C.P., Carpousis, A.J., and Krisch, H.M. (1992) Specificity of Escherichia coli endoribonuclease RNase E: in vivo and in vitro analysis of mutants in a bacteriophage T4 mRNA processing site. Genes Dev. 6, 149-159
    • (1992) Genes Dev. , vol.6 , pp. 149-159
    • Ehretsmann, C.P.1    Carpousis, A.J.2    Krisch, H.M.3
  • 16
    • 0028341449 scopus 로고
    • A+U content rather than a particular nucleotide order determines the specificity of RNase E cleavage
    • McDowall, K.J., Lin-Chao, S., and Cohen, S.N. (1994) A+U content rather than a particular nucleotide order determines the specificity of RNase E cleavage. J. Biol. Chem. 269, 10790-10796
    • (1994) J. Biol. Chem. , vol.269 , pp. 10790-10796
    • McDowall, K.J.1    Lin-Chao, S.2    Cohen, S.N.3
  • 17
    • 0028276973 scopus 로고
    • Effects of nucleotide sequence on the specificity of rne-dependent and RNase E-mediated cleavages of RNA I encoded by the pBR322 plasmid
    • Lin-Chao, S., Wong, T.T., McDowall, K.J., and Cohen, S.N. (1994) Effects of nucleotide sequence on the specificity of rne-dependent and RNase E-mediated cleavages of RNA I encoded by the pBR322 plasmid. J. Biol. Chem. 269, 10797-10803
    • (1994) J. Biol. Chem. , vol.269 , pp. 10797-10803
    • Lin-Chao, S.1    Wong, T.T.2    McDowall, K.J.3    Cohen, S.N.4
  • 18
    • 0025796969 scopus 로고
    • Specific endonucleolytic cleavage of the mRNA for ribosomal protein S20 of Escherichia coli requires the product of the ams gene in vivo and in vitro
    • Mackie, G.A. (1991) Specific endonucleolytic cleavage of the mRNA for ribosomal protein S20 of Escherichia coli requires the product of the ams gene in vivo and in vitro. J. Bacteriol. 173, 2488-2497
    • (1991) J. Bacteriol. , vol.173 , pp. 2488-2497
    • Mackie, G.A.1
  • 19
    • 0020025040 scopus 로고
    • Processing of bacteriophage T4 transfer RNAs. Structural analysis and in vitro processing of precursors that accumulate in RNase E-strains
    • Pragai, B. and Apirion, D. (1982) Processing of bacteriophage T4 transfer RNAs. Structural analysis and in vitro processing of precursors that accumulate in RNase E-strains. J. Mol. Biol. 154, 465-484
    • (1982) J. Mol. Biol. , vol.154 , pp. 465-484
    • Pragai, B.1    Apirion, D.2
  • 20
    • 0026557264 scopus 로고
    • Secondary structure of the mRNA for ribosomeal protein S20
    • Mackie, G.A. (1992) Secondary structure of the mRNA for ribosomeal protein S20. J. Biol. Chem. 267, 1054-1061
    • (1992) J. Biol. Chem. , vol.267 , pp. 1054-1061
    • Mackie, G.A.1
  • 21
    • 0027717298 scopus 로고
    • The role of RNA structure in determining RNase E-dependent cleavage sites in the mRNA for ribosomal protein S20 in vitro
    • Mackie, G.A. and Genereaux, J.L. (1993) The role of RNA structure in determining RNase E-dependent cleavage sites in the mRNA for ribosomal protein S20 in vitro. J. Mol. Biol. 234, 998-1012
    • (1993) J. Mol. Biol. , vol.234 , pp. 998-1012
    • Mackie, G.A.1    Genereaux, J.L.2
  • 22
    • 0024043391 scopus 로고
    • In vivo and in vitro identity of site specific cleavages in the 5′ non-coding region of ompA and bal mRNAs in Escherichia coli
    • Nilsson, G., Lundberg, U., and von Gabain, A. (1988) In vivo and in vitro identity of site specific cleavages in the 5′ non-coding region of ompA and bal mRNAs in Escherichia coli. EMBO J. 7, 2269-2275
    • (1988) EMBO J. , vol.7 , pp. 2269-2275
    • Nilsson, G.1    Lundberg, U.2    Von Gabain, A.3
  • 23
    • 0027054379 scopus 로고
    • Structural requirements for the processing of Escherichia coli 5S ribosomal RNA by RNase E in vitro
    • Cormack, R.S. and Mackie, G.A. (1992) Structural requirements for the processing of Escherichia coli 5S ribosomal RNA by RNase E in vitro. J. Mol. Biol. 228, 1078-1090
    • (1992) J. Mol. Biol. , vol.228 , pp. 1078-1090
    • Cormack, R.S.1    Mackie, G.A.2
  • 24
    • 0031031467 scopus 로고    scopus 로고
    • Modulation of the activity of RNase E in vitro by RNA sequences and secondary structures 5′ to cleavage sites
    • Mackie, G.A., Genereaux, J.L., and Masterman, S.K. (1997) Modulation of the activity of RNase E in vitro by RNA sequences and secondary structures 5′ to cleavage sites. J. Biol. Chem. 272, 609-616
    • (1997) J. Biol. Chem. , vol.272 , pp. 609-616
    • Mackie, G.A.1    Genereaux, J.L.2    Masterman, S.K.3
  • 25
    • 0028987956 scopus 로고
    • Site-specific RNase E cleavage of oligonucleotides and inhibition by stem-loops
    • McDowall, K.J., Kaberdin, V.R., Wu, S.-W., Cohen, S.N., and Lin-Chao, S. (1995) Site-specific RNase E cleavage of oligonucleotides and inhibition by stem-loops. Nature 374, 287-290
    • (1995) Nature , vol.374 , pp. 287-290
    • McDowall, K.J.1    Kaberdin, V.R.2    Wu, S.-W.3    Cohen, S.N.4    Lin-Chao, S.5
  • 26
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of enzyme
    • Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., and Altman, S. (1983) The RNA moiety of ribonuclease P is the catalytic subunit of enzyme. Cell 35, 849-857
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 27
    • 0020788634 scopus 로고
    • Identification of a precursor molecular for the RNA moiety of the processing enzyme RNase P
    • Gurevitz, M., Jain, S.K., and Apirion, D. (1983) Identification of a precursor molecular for the RNA moiety of the processing enzyme RNase P. Proc. Natl Acad. Sci. USA 80, 4450-4454
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 4450-4454
    • Gurevitz, M.1    Jain, S.K.2    Apirion, D.3
  • 28
    • 0003331562 scopus 로고
    • Processing of transcription products of the gene encoding the RNA component of RNase P
    • Sakamoto, H., Kimura, N., and Shimura, Y. (1983) Processing of transcription products of the gene encoding the RNA component of RNase P. Proc. Natl Acad. Sci. USA 80, 6187-6191
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 6187-6191
    • Sakamoto, H.1    Kimura, N.2    Shimura, Y.3
  • 29
    • 0029295957 scopus 로고
    • Processing of the precursor to the catalytic RNA subunit of RNase P from Escherichia coli
    • Lundberg, U. and Altman, S. (1995) Processing of the precursor to the catalytic RNA subunit of RNase P from Escherichia coli. RNA 1, 327-334
    • (1995) RNA , vol.1 , pp. 327-334
    • Lundberg, U.1    Altman, S.2
  • 30
    • 0029765533 scopus 로고    scopus 로고
    • Mutational analysis of RNA structures and sequences postulated to affect 3′ processing of M1 RNA, the RNA component of Escherichia coli RNase P
    • Kim, S., Kim, H., Park, I., and Lee, Y. (1996) Mutational analysis of RNA structures and sequences postulated to affect 3′ processing of M1 RNA, the RNA component of Escherichia coli RNase P. J. Biol. Chem. 271, 19330-19337
    • (1996) J. Biol. Chem. , vol.271 , pp. 19330-19337
    • Kim, S.1    Kim, H.2    Park, I.3    Lee, Y.4
  • 31
    • 0033081246 scopus 로고    scopus 로고
    • In vitro analysis of processing at the 3′-end of precursors of Ml RNA, the catalytic subunit of Escherichia coli RNase P: Multiple pathways and steps for the processing
    • Kim, S., Sim, S., and Lee, Y. (1999) In vitro analysis of processing at the 3′-end of precursors of Ml RNA, the catalytic subunit of Escherichia coli RNase P: multiple pathways and steps for the processing. Nucleic Acids Res. 27, 895-901
    • (1999) Nucleic Acids Res. , vol.27 , pp. 895-901
    • Kim, S.1    Sim, S.2    Lee, Y.3
  • 32
    • 0037048524 scopus 로고    scopus 로고
    • 3′-end processing of precursor Ml RNA by the N-terminal half of RNase E
    • Sim, S., Kim, K., and Lee, Y. (2002) 3′-end processing of precursor Ml RNA by the N-terminal half of RNase E. FEBS Lett. 529, 225-231
    • (2002) FEBS Lett. , vol.529 , pp. 225-231
    • Sim, S.1    Kim, K.2    Lee, Y.3
  • 33
    • 0035860370 scopus 로고    scopus 로고
    • Role of the sequence of the rne-dependent site in 3′ processing of M1 RNA, the catalytic component of Escherichia coli RNase P
    • Sim, S., Kim, S., and Lee, Y. (2001) Role of the sequence of the rne-dependent site in 3′ processing of M1 RNA, the catalytic component of Escherichia coli RNase P. FEBS Lett. 505, 291-295
    • (2001) FEBS Lett. , vol.505 , pp. 291-295
    • Sim, S.1    Kim, S.2    Lee, Y.3
  • 34
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 33, 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 37
    • 0034636985 scopus 로고    scopus 로고
    • Enhanced cleavage of RNA mediated by an interaction between substrates and the arginine-rich domain of E. coli ribonuclease E
    • Kaberdin, V.R., Walsh, A.P., Jakobsen, T., McDowall, K.J., and von Gabain, A. (2000) Enhanced cleavage of RNA mediated by an interaction between substrates and the arginine-rich domain of E. coli ribonuclease E. J. Mol. Biol. 301, 257-264
    • (2000) J. Mol. Biol. , vol.301 , pp. 257-264
    • Kaberdin, V.R.1    Walsh, A.P.2    Jakobsen, T.3    McDowall, K.J.4    Von Gabain, A.5
  • 38
    • 0242395917 scopus 로고    scopus 로고
    • Probing the substrate specificity of Escherichia coli RNase E using a novel oligonucleotide-based assay
    • Kaberdin, V.R. (2003) Probing the substrate specificity of Escherichia coli RNase E using a novel oligonucleotide-based assay. Nucl. Acids Res. 31, 4710-4716
    • (2003) Nucl. Acids Res. , vol.31 , pp. 4710-4716
    • Kaberdin, V.R.1
  • 39
    • 0016232066 scopus 로고
    • Catalysis, binding and enzyme-substrate complementarity
    • Fersht, A.R. (1974) Catalysis, binding and enzyme-substrate complementarity. Proc. R. Soc. Lond. B Biol. Sci. 187, 397-407
    • (1974) Proc. R. Soc. Lond. B Biol. Sci. , vol.187 , pp. 397-407
    • Fersht, A.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.