메뉴 건너뛰기




Volumn 13, Issue 19, 1999, Pages 2594-2603

Reconstitution of a minimal RNA degradosome demonstrates functional coordination between a 3 exonuclease and a DEAD-box RNA helicase

Author keywords

3' exonuclease; DEAD box; E. coli; RNA degradosome; RNA helicase

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL RNA; EXODEOXYRIBONUCLEASE III; RNA HELICASE;

EID: 0033214259     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.13.19.2594     Document Type: Article
Times cited : (155)

References (41)
  • 1
    • 0032489015 scopus 로고    scopus 로고
    • The cell as a collection of protein machines: Preparing the next generation of molecular biologists
    • Alberts, B. 1998. The cell as a collection of protein machines: Preparing the next generation of molecular biologists. Cell 92: 291-294.
    • (1998) Cell , vol.92 , pp. 291-294
    • Alberts, B.1
  • 2
    • 0000577868 scopus 로고    scopus 로고
    • The 3′ to 5′ degradation of yeast mRNA is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex
    • Anderson, J.S.J. and R. Parker. 1998. The 3′ to 5′ degradation of yeast mRNA is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3′ to 5′ exonucleases of the exosome complex. EMBO J. 17: 1497-1506.
    • (1998) EMBO J. , vol.17 , pp. 1497-1506
    • Anderson, J.S.J.1    Parker, R.2
  • 3
    • 0030779484 scopus 로고    scopus 로고
    • Polyphosphate kinase is a component of the Escherichia coli RNA degradosome
    • Blum, E., B. Py, A.J. Carpousis, and C.F. Higgins. 1997. Polyphosphate kinase is a component of the Escherichia coli RNA degradosome. Mol. Microbiol. 26: 387-398.
    • (1997) Mol. Microbiol. , vol.26 , pp. 387-398
    • Blum, E.1    Py, B.2    Carpousis, A.J.3    Higgins, C.F.4
  • 4
    • 0033548140 scopus 로고    scopus 로고
    • Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro
    • Blum, E., A.J. Carpousis, and C.F. Higgins. 1999. Polyadenylation promotes degradation of 3′-structured RNA by the Escherichia coli mRNA degradosome in vitro. J. Biol. Chem. 274: 4009-4016.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4009-4016
    • Blum, E.1    Carpousis, A.J.2    Higgins, C.F.3
  • 5
    • 0028269435 scopus 로고
    • Copurification of E. coli RNase E and PNPase: Evidence for a specific association between two enzymes important for RNA processing and degradation
    • Carpousis, A.J., G. Van Houwe, C. Ehretsmann, and H.M. Krisch. 1994. Copurification of E. coli RNase E and PNPase: Evidence for a specific association between two enzymes important for RNA processing and degradation. Cell 76: 889-900.
    • (1994) Cell , vol.76 , pp. 889-900
    • Carpousis, A.J.1    Van Houwe, G.2    Ehretsmann, C.3    Krisch, H.M.4
  • 6
    • 0030041546 scopus 로고    scopus 로고
    • Overexpression, purification and properties of Escherichia coli ribonuclease II
    • Coburn, G.A. and G.A. Mackie. 1996a. Overexpression, purification and properties of Escherichia coli ribonuclease II. J. Biol. Chem. 271: 1048-1053.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1048-1053
    • Coburn, G.A.1    Mackie, G.A.2
  • 7
    • 0029945427 scopus 로고    scopus 로고
    • Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3′-exonucleases dependent on oligoadenylation and RNA secondary structure
    • _. 1996b. Differential sensitivities of portions of the mRNA for ribosomal protein S20 to 3′-exonucleases dependent on oligoadenylation and RNA secondary structure. J. Biol. Chem. 271: 15776-15781.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15776-15781
  • 8
    • 0032569032 scopus 로고    scopus 로고
    • Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes
    • _. 1998. Reconstitution of the degradation of the mRNA for ribosomal protein S20 with purified enzymes. J. Mol. Biol. 279: 1061-1074.
    • (1998) J. Mol. Biol. , vol.279 , pp. 1061-1074
  • 9
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • _. 1999. Degradation of mRNA in Escherichia coli: An old problem with some new twists. Prog. Nucleic Acids Res. Mol. Biol. 62: 55-108.
    • (1999) Prog. Nucleic Acids Res. Mol. Biol. , vol.62 , pp. 55-108
  • 10
    • 0027054379 scopus 로고
    • Structural requirements for the processing of Escherichia coli 5S ribosomal RNA by RNase E in vitro
    • Cormack, R.S. and G.A. Mackie. 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
  • 11
    • 0027380985 scopus 로고
    • RNase E activity is conferred by a single polypeptide: Overexpression, purification and properties of the ams/rne/hmp-1 gene product
    • Cormack, R.S., J.L. Genereaux, and G.A. Mackie. 1993. RNase E activity is conferred by a single polypeptide: Overexpression, purification and properties of the ams/rne/hmp-1 gene product. Proc. Natl. Acad. Sci. 90: 9006-9010.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 9006-9010
    • Cormack, R.S.1    Genereaux, J.L.2    Mackie, G.A.3
  • 12
    • 0032481316 scopus 로고    scopus 로고
    • Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for 3′ end formation of 5.8S rRNA in Saccharomyces cerevisiae
    • de la Cruz, J., D. Kressler, D. Tollervey, and P. Linder. 1998. Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for 3′ end formation of 5.8S rRNA in Saccharomyces cerevisiae. EMBO J. 17: 1128-1140.
    • (1998) EMBO J. , vol.17 , pp. 1128-1140
    • De La Cruz, J.1    Kressler, D.2    Tollervey, D.3    Linder, P.4
  • 13
    • 0033066929 scopus 로고    scopus 로고
    • A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli
    • García-Mena, J., A. Das, A. Sánchez-Trujillo, C. Portier, and C. Montañez. 1999. A novel mutation in the KH domain of polynucleotide phosphorylase affects autoregulation and mRNA decay in Escherichia coli. Mol. Microbiol. 33: 235-248.
    • (1999) Mol. Microbiol. , vol.33 , pp. 235-248
    • García-Mena, J.1    Das, A.2    Sánchez-Trujillo, A.3    Portier, C.4    Montañez, C.5
  • 14
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA-binding proteins
    • Hayes, R., J. Kudla, G. Schuster, L. Gabay, P. Maliga, and W. Gruissem. 1996. Chloroplast mRNA 3′-end processing by a high molecular weight protein complex is regulated by nuclear encoded RNA-binding proteins. EMBO J. 15: 1132-1141.
    • (1996) EMBO J. , vol.15 , pp. 1132-1141
    • Hayes, R.1    Kudla, J.2    Schuster, G.3    Gabay, L.4    Maliga, P.5    Gruissem, W.6
  • 15
    • 0025943266 scopus 로고
    • rh1B, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a procaryote
    • Kalman, M., H. Murphy, and M. Cashel. 1991. rh1B, a new Escherichia coli K-12 gene with an RNA helicase-like protein sequence motif, one of at least five such possible genes in a procaryote. New Biologist 3: 886-895.
    • (1991) New Biologist , vol.3 , pp. 886-895
    • Kalman, M.1    Murphy, H.2    Cashel, M.3
  • 16
    • 0344741924 scopus 로고    scopus 로고
    • RNase E polypeptides lacking the carboxy-terminal half suppress a mukB mutation in Escherichia coli
    • Kido, M., K. Yamanaka, T. Mitani, H. Niki, T. Ogura, and S. Hiraga. 1996. RNase E polypeptides lacking the carboxy-terminal half suppress a mukB mutation in Escherichia coli. J. Bacteriol. 177: 491-496.
    • (1996) J. Bacteriol. , vol.177 , pp. 491-496
    • Kido, M.1    Yamanaka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6
  • 17
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structure of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., J. Hsieh, G.H. Gauss, T.M. Lohman, and G. Waksman. 1997. Major domain swiveling revealed by the crystal structure of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90: 635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 18
    • 0033048415 scopus 로고    scopus 로고
    • The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo
    • Lopez, P.J., I. Marchand, S.A. Joyce, and M. Dreyfus. 1999. The C-terminal half of RNase E, which organizes the Escherichia coli degradosome, participates in mRNA degradation but not rRNA processing in vivo. Mol. Microbiol. 33: 188-199.
    • (1999) Mol. Microbiol. , vol.33 , pp. 188-199
    • Lopez, P.J.1    Marchand, I.2    Joyce, S.A.3    Dreyfus, M.4
  • 19
    • 0024720429 scopus 로고
    • Stabilization of the 3′ one-third of Escherichia coli ribosomal protein S20 mRNA in mutants lacking polynucleotide phosphorylase
    • Mackie, G.A. 1989. Stabilization of the 3′ one-third of Escherichia coli ribosomal protein S20 mRNA in mutants lacking polynucleotide phosphorylase. J. Bacteriol. 171: 4112-4120.
    • (1989) J. Bacteriol. , vol.171 , pp. 4112-4120
    • Mackie, G.A.1
  • 20
    • 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
    • _. 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
  • 21
    • 0032531768 scopus 로고    scopus 로고
    • Ribonuclease E is a 5′-end-dependent endonuclease
    • _. 1998. Ribonuclease E is a 5′-end-dependent endonuclease. Nature 395: 720-723.
    • (1998) Nature , vol.395 , pp. 720-723
  • 22
    • 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 J.L. Genereaux. 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
  • 23
    • 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., J.L. Genereaux, and S.K. Masterman. 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
  • 24
    • 0030034498 scopus 로고    scopus 로고
    • The DexH box protein Suv3p is a component of a yeast mitochondrial 3′ to 5′ exonuclease complex that suppresses group I intron toxicity
    • Margossian, S.P., H. Li, H.P. Zassenhaus, and H.P. Butow. 1996. The DexH box protein Suv3p is a component of a yeast mitochondrial 3′ to 5′ exonuclease complex that suppresses group I intron toxicity. Cell 84: 199-209.
    • (1996) Cell , vol.84 , pp. 199-209
    • Margossian, S.P.1    Li, H.2    Zassenhaus, H.P.3    Butow, H.P.4
  • 25
    • 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 S.N. Cohen. 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
  • 26
    • 0025740223 scopus 로고
    • mRNA degradation by processive 3′-exoribonucleases in vitro and the implication for mRNA decay in vivo
    • McLaren, R.S., S.F. Newbury, G.S.C. Dance, H.C. Causton, and C.F. Higgins. 1991. mRNA degradation by processive 3′-exoribonucleases in vitro and the implication for mRNA decay in vivo. J. Mol. Biol. 221: 81-95.
    • (1991) J. Mol. Biol. , vol.221 , pp. 81-95
    • McLaren, R.S.1    Newbury, S.F.2    Dance, G.S.C.3    Causton, H.C.4    Higgins, C.F.5
  • 27
    • 0029976430 scopus 로고    scopus 로고
    • Proteins associated with RNase E in a multicomponent ribonucleolytic complex
    • Miczak, A., V.R. Kaberdin, C.L. Wei, and S. Lin-Chao. 1996. Proteins associated with RNase E in a multicomponent ribonucleolytic complex. Proc. Natl. Acad. Sci. 93: 3865-3869.
    • (1996) Proc. Natl. Acad. Sci. , vol.93 , pp. 3865-3869
    • Miczak, A.1    Kaberdin, V.R.2    Wei, C.L.3    Lin-Chao, S.4
  • 28
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′-5′ exoribonucleases
    • Mitchell, P., E. Petfalski, A. Shevchenko, M. Mann, and D. Tollervey. 1997. The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′-5′ exoribonucleases. Cell 91: 457-466.
    • (1997) Cell , vol.91 , pp. 457-466
    • Mitchell, P.1    Petfalski, E.2    Shevchenko, A.3    Mann, M.4    Tollervey, D.5
  • 29
    • 0027945686 scopus 로고
    • A protein complex mediating mRNA turnover in Escherichia coli
    • Py, B., H. Causton, E.A. Mudd, and C.F. Higgins. 1994. A protein complex mediating mRNA turnover in Escherichia coli. Mol. Microbiol. 14: 717-729.
    • (1994) Mol. Microbiol. , vol.14 , pp. 717-729
    • Py, B.1    Causton, H.2    Mudd, E.A.3    Higgins, C.F.4
  • 30
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py, B., C.F. Higgins, and A.J. Carpousis. 1996. A DEAD-box RNA helicase in the Escherichia coli RNA degradosome. Nature 381: 169-172.
    • (1996) Nature , vol.381 , pp. 169-172
    • Py, B.1    Higgins, C.F.2    Carpousis, A.J.3
  • 31
    • 0014477758 scopus 로고
    • Isolation and mapping of polynucleotide phosphorylase mutants of Escherichia coli
    • Reiner, A.M. 1969. Isolation and mapping of polynucleotide phosphorylase mutants of Escherichia coli. J. Bacteriol. 97: 1431-1436.
    • (1969) J. Bacteriol. , vol.97 , pp. 1431-1436
    • Reiner, A.M.1
  • 32
    • 0027990470 scopus 로고
    • Purification, properties, and subcellular localization of foxtail mosaic potexvirus 26-kDa protein
    • Rouleau, M., R.J. Smith, J.B. Bancroft, and G.A. Mackie. 1994. Purification, properties, and subcellular localization of foxtail mosaic potexvirus 26-kDa protein. Virology 204: 254-265.
    • (1994) Virology , vol.204 , pp. 254-265
    • Rouleau, M.1    Smith, R.J.2    Bancroft, J.B.3    Mackie, G.A.4
  • 33
    • 0004136246 scopus 로고
    • ed. N. Ford, C. Nolan, and M. Ferguson. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., E.F. Fritsch, and T. Maniatis. 1989. In Molecular cloning: A laboratory manual (ed. N. Ford, C. Nolan, and M. Ferguson). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Molecular Cloning: A Laboratory Manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 34
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicases
    • Schmid, S.R. and P. Linder. 1992. D-E-A-D protein family of putative RNA helicases. Mol. Microbiol. 6: 283-292.
    • (1992) Mol. Microbiol. , vol.6 , pp. 283-292
    • Schmid, S.R.1    Linder, P.2
  • 36
    • 0028840292 scopus 로고
    • Evidence for an RNA-binding region in the Escherichia coli processing endoribonuclease RNase E
    • Taraseviciene, L., G.R. Björk, and B.E. Uhlin. 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    Björk, G.R.2    Uhlin, B.E.3
  • 38
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velanker, S.S., P. Soultanas, M.S. Dillingham, H.S. Subramanya, and D.E. Wigley. 1999. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97: 75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velanker, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.E.5
  • 39
    • 0026546001 scopus 로고
    • Allosteric effects of nucleotide cofactors on Escherichia coli REP helicase-DNA binding
    • Wong, I. and T.M. Lohman. 1992. Allosteric effects of nucleotide cofactors on Escherichia coli REP helicase-DNA binding. Science 256: 350-355.
    • (1992) Science , vol.256 , pp. 350-355
    • Wong, I.1    Lohman, T.M.2
  • 40
    • 0028945837 scopus 로고
    • RNA degradation in Escherichia coli is regulated by 3′-adenylation and 5′-phosphorylation
    • Xu, F. and S.N. Cohen. 1995. RNA degradation in Escherichia coli is regulated by 3′-adenylation and 5′-phosphorylation. Nature 374: 180-183.
    • (1995) Nature , vol.374 , pp. 180-183
    • Xu, F.1    Cohen, S.N.2
  • 41
    • 0018353521 scopus 로고
    • Enzyme-catalyzed DNA unwinding: Studies on Escherichia coli rep DNA helicase
    • Yarranton, G.T. and M.L. Gefter. 1979. Enzyme-catalyzed DNA unwinding: Studies on Escherichia coli rep DNA helicase. Proc. Natl. Acad. Sci. 76: 1658-1662.
    • (1979) Proc. Natl. Acad. Sci. , vol.76 , pp. 1658-1662
    • Yarranton, G.T.1    Gefter, M.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.