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Volumn 12, Issue 17, 1998, Pages 2770-2781

Ribonuclease E organizes the protein interactions in the Escherichia coli RNA degradosome

Author keywords

DEAD box RNA helicase; Protein protein interactions; RhlB activation; Ribonuclease E; RNA degradation; RNA degradosome

Indexed keywords

BACTERIAL RNA; RIBONUCLEASE;

EID: 3543037550     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.12.17.2770     Document Type: Article
Times cited : (285)

References (52)
  • 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
    • 0024244201 scopus 로고
    • Mechanisms of mRNA decay in bacteria: A perspective
    • Belasco, J.G. and C.F. Higgins. 1988. Mechanisms of mRNA decay in bacteria: A perspective. Gene 72: 15-23.
    • (1988) Gene , vol.72 , pp. 15-23
    • Belasco, J.G.1    Higgins, C.F.2
  • 4
    • 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
  • 5
    • 0029961542 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is required for the rapid degradation of the RNase E-processed rpsO mRNA of Escherichia coli devoid of its 3′ hairpin
    • Braun, F., E. Hajnsdorf, and P. Régnier. 1996. Polynucleotide phosphorylase is required for the rapid degradation of the RNase E-processed rpsO mRNA of Escherichia coli devoid of its 3′ hairpin. Mol. Microbiol. 19: 997-1005.
    • (1996) Mol. Microbiol. , vol.19 , pp. 997-1005
    • Braun, F.1    Hajnsdorf, E.2    Régnier, P.3
  • 6
    • 0028269435 scopus 로고
    • Copurification of E. coli RNase E and PNPase: Evidence for a specific association between two enzymes important in 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 in 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
  • 7
    • 0026447906 scopus 로고
    • Cloning and analysis of the entire E. coli ams gene. Ams is identical to hmp1 and encodes a 114 kDa protein that migrates as a 180 kDa protein
    • Corrigendum 238: 867
    • Casarégola, S., A. Jacq, D. Laoudj, G. McGurk, S. Margarson, M. Tempête, V. Norris, and I.B. Holland. 1992. Cloning and analysis of the entire E. 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. [Corrigendum 238: 867.]
    • (1992) J. Mol. Biol. , vol.228 , pp. 30-40
    • Casarégola, S.1    Jacq, A.2    Laoudj, D.3    McGurk, G.4    Margarson, S.5    Tempête, M.6    Norris, V.7    Holland, I.B.8
  • 8
    • 0028261194 scopus 로고
    • Effective amplification of long targets from cloned inserts and human genomic DNA
    • Cheng, S., C. Fockler, W.M. Barnes, and R. Higuchi. 1994. Effective amplification of long targets from cloned inserts and human genomic DNA. Proc. Natl. Acad. Sci. 91: 5695-5699.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 5695-5699
    • Cheng, S.1    Fockler, C.2    Barnes, W.M.3    Higuchi, R.4
  • 9
    • 0021714276 scopus 로고
    • A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors
    • Churchward, G., D. Belin, and Y. Nagamine. 1984. A pSC101-derived plasmid which shows no sequence homology to other commonly used cloning vectors. Gene 31: 165-171.
    • (1984) Gene , vol.31 , pp. 165-171
    • Churchward, G.1    Belin, D.2    Nagamine, Y.3
  • 11
    • 0028923019 scopus 로고
    • Surprises at the 3′ end of prokaryotic RNA
    • Cohen, S.N. 1995. Surprises at the 3′ end of prokaryotic RNA. Cell 80: 829-832.
    • (1995) Cell , vol.80 , pp. 829-832
    • Cohen, S.N.1
  • 12
    • 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
  • 13
    • 0028225930 scopus 로고
    • Plasmid pSC101 harbors a recombination site, psi, which is able to resolve plasmid multimers and to substitute for the analogous chromosomal Escherichia coli site dif
    • Cornet, F., I. Mortier, J. Patte, and J.M. Louarn. 1994. Plasmid pSC101 harbors a recombination site, psi, which is able to resolve plasmid multimers and to substitute for the analogous chromosomal Escherichia coli site dif. J. Bact. 176: 3188-3195.
    • (1994) J. Bact. , vol.176 , pp. 3188-3195
    • Cornet, F.1    Mortier, I.2    Patte, J.3    Louarn, J.M.4
  • 14
    • 0032481316 scopus 로고    scopus 로고
    • Dob1p (Mtr4p) is a putative ATP-dependent RNA helicase required for the 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 the 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
  • 15
    • 0022553775 scopus 로고
    • Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies
    • Dunn, S.D. 1986. Effects of the modification of transfer buffer composition and the renaturation of proteins in gels on the recognition of proteins on Western blots by monoclonal antibodies. Anal. Biochem. 157: 144-153.
    • (1986) Anal. Biochem. , vol.157 , pp. 144-153
    • Dunn, S.D.1
  • 16
    • 0026666319 scopus 로고
    • Messenger RNA degradation in procaryotes
    • Ehretsmann, C., A.J. Carpousis, and H.M. Krisch. 1992. Messenger RNA degradation in procaryotes. FASEB J. 6: 3186-3192.
    • (1992) FASEB J. , vol.6 , pp. 3186-3192
    • Ehretsmann, C.1    Carpousis, A.J.2    Krisch, H.M.3
  • 17
    • 0024059423 scopus 로고
    • A simple method for predicting the secondary structure of globular proteins: Implications and accuracy
    • Gascuel, O. and J.L. Golmard. 1988. A simple method for predicting the secondary structure of globular proteins: Implications and accuracy. Comput. Appl. Biosci. 4: 357-365.
    • (1988) Comput. Appl. Biosci. , vol.4 , pp. 357-365
    • Gascuel, O.1    Golmard, J.L.2
  • 18
    • 0025233327 scopus 로고
    • Preparation of extracts from plants
    • Gegenheimer, P. 1990. Preparation of extracts from plants. Methods Enzymol. 182: 174-193.
    • (1990) Methods Enzymol. , vol.182 , pp. 174-193
    • Gegenheimer, P.1
  • 19
    • 0028285542 scopus 로고
    • Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: Implications for monomeric RNA helicases
    • Gibson, T.J. and J.D. Thompson. 1994. Detection of dsRNA-binding domains in RNA helicase A and Drosophila maleless: Implications for monomeric RNA helicases. Nucleic Acids Res. 22: 2552-2556.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2552-2556
    • Gibson, T.J.1    Thompson, J.D.2
  • 20
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R.A. Woods, and R.H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20: 1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 21
    • 0002337352 scopus 로고
    • Interaction trap/two hyhrid system to identify interacting proteins
    • (ed. F.M. Ausubel), Wiley, New York, NY
    • Golemis, E.A., J. Gyuris, and R. Brent. 1994. Interaction trap/two hyhrid system to identify interacting proteins. In Current protocols in molecular biology (ed. F.M. Ausubel), Vol. 2, 13-14. Wiley, New York, NY.
    • (1994) Current Protocols in Molecular Biology , vol.2 , pp. 13-14
    • Golemis, E.A.1    Gyuris, J.2    Brent, R.3
  • 22
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phophatase that associates with Cdk2
    • Gyuris, J., E.A. Golemis, H. Chertkov, and R. Brent. 1993. Cdi1, a human G1 and S phase protein phophatase that associates with Cdk2. Cell 75: 791-803.
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.A.2    Chertkov, H.3    Brent, R.4
  • 23
    • 0029917715 scopus 로고    scopus 로고
    • Chloroplast mRNA 3′-end processing by a high molecular 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 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
  • 24
    • 0024357799 scopus 로고
    • A simple method for site-directed mutagenesis using the polymerase chain reaction
    • Hemsley, A., N. Arnheim, M.D. Toney, G. Cortopassi, and D.J. Galas. 1989. A simple method for site-directed mutagenesis using the polymerase chain reaction. Nucleic Acids Res. 17: 6545-6551.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 6545-6551
    • Hemsley, A.1    Arnheim, N.2    Toney, M.D.3    Cortopassi, G.4    Galas, D.J.5
  • 25
    • 0031952026 scopus 로고    scopus 로고
    • Poly(A)- and poly(U)-specific RNA 3′ tail shortening by E. coli ribonuclease E
    • Huang, H., J. Liao, and S.N. Cohen. 1998. Poly(A)-and poly(U)-specific RNA 3′ tail shortening by E. coli ribonuclease E. Nature 391: 99-102.
    • (1998) Nature , vol.391 , pp. 99-102
    • Huang, H.1    Liao, J.2    Cohen, S.N.3
  • 26
    • 0028797303 scopus 로고
    • RNase E auto-regulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: Unusual sensitivity of the rne transcript to RNase E activity
    • Jain, C. and J.G. Belasco. 1995. RNase E auto-regulates its synthesis by controlling the degradation rate of its own mRNA in Escherichia coli: Unusual sensitivity of the rne transcript to RNase E activity. Genes & Dev. 9: 84-96.
    • (1995) Genes & Dev. , vol.9 , pp. 84-96
    • Jain, C.1    Belasco, J.G.2
  • 27
    • 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 prokaryote
    • 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 prokaryote. New Biologist 3: 886-895.
    • (1991) New Biologist , vol.3 , pp. 886-895
    • Kalman, M.1    Murphy, H.2    Cashel, M.3
  • 28
    • 0029889965 scopus 로고    scopus 로고
    • RNase E polypeptides lacking a carboxyl-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 a carboxyl-terminal half suppress a mukB mutation in Escherichia coli. J. Bacteriol. 178: 3917-3925.
    • (1996) J. Bacteriol. , vol.178 , pp. 3917-3925
    • Kido, M.1    Yamanaka, K.2    Mitani, T.3    Niki, H.4    Ogura, T.5    Hiraga, S.6
  • 29
    • 0018604988 scopus 로고
    • Conditionally lethal amber mutations in the dnaA region of the Escherichia coli chromosome that affect chromosome replication
    • Kimura, M., T. Miki, S. Hiraga, T. Nagata, and T. Yura. 1979. Conditionally lethal amber mutations in the dnaA region of the Escherichia coli chromosome that affect chromosome replication. J. Bacteriol. 140: 825-834.
    • (1979) J. Bacteriol. , vol.140 , pp. 825-834
    • Kimura, M.1    Miki, T.2    Hiraga, S.3    Nagata, T.4    Yura, T.5
  • 30
    • 77956896894 scopus 로고
    • Polynucleotide phosphorylase
    • Littauer, U.Z. and H. Soreq. 1982. Polynucleotide phosphorylase. Enzymes 15: 517-533.
    • (1982) Enzymes , vol.15 , pp. 517-533
    • Littauer, U.Z.1    Soreq, H.2
  • 31
    • 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
  • 32
    • 0030034498 scopus 로고    scopus 로고
    • The DExH box protein Suv3p is a component of a yeast mitochondrial 3′ to 5′ exoribonuclease that suppresses group I intron toxicity
    • Margossian, S.P., H. Li, H.P. Zassenhaus, and R.A. Butow. 1996. The DExH box protein Suv3p is a component of a yeast mitochondrial 3′ to 5′ exoribonuclease 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, R.A.4
  • 33
    • 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
  • 34
    • 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
  • 35
    • 0024998982 scopus 로고
    • Cloning and expression of eukaryotic initiation factor 4B cDNA: Sequence determination identifies a common RNA recognition motif
    • Milburn, S.C., J.W.B. Hershey, M.V. Davies, K. Kelleher, and R.J. Kaufman. 1990. Cloning and expression of eukaryotic initiation factor 4B cDNA: Sequence determination identifies a common RNA recognition motif. EMBO J. 9: 2783-2790.
    • (1990) EMBO J. , vol.9 , pp. 2783-2790
    • Milburn, S.C.1    Hershey, J.W.B.2    Davies, M.V.3    Kelleher, K.4    Kaufman, R.J.5
  • 36
    • 0030702085 scopus 로고    scopus 로고
    • The exosome: A conserved eukaryotic RNA processing complex containing multiple 3′-5′ exoribonucleases
    • Mitchell, P., E. Petfalski, A. Shevchenku, 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    Shevchenku, A.3    Mann, M.4    Tollervey, D.5
  • 37
    • 0031588902 scopus 로고    scopus 로고
    • The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4
    • Monod, C., F. Repoila, M. Kutateladze, F. Tétart, and H.M. Krisch. 1997. The genome of the pseudo T-even bacteriophages, a diverse group that resembles T4. J. Mol. Biol. 267: 237-249.
    • (1997) J. Mol. Biol. , vol.267 , pp. 237-249
    • Monod, C.1    Repoila, F.2    Kutateladze, M.3    Tétart, F.4    Krisch, H.M.5
  • 38
    • 0025688893 scopus 로고
    • RNase E, and 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., H.M. Krisch, and C.F. Higgins. 1990. RNase E, and 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
  • 40
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF4A
    • Pause, A. and N. Sonenberg. 1992. Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF4A. EMBO J. 11: 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 41
    • 0016705035 scopus 로고
    • Quaternary structure of polynucleotide phosphorylase from E. coli: Evidence for a complex between two types of polypeptide chains
    • Portier, C. 1975. Quaternary structure of polynucleotide phosphorylase from E. coli: Evidence for a complex between two types of polypeptide chains. Eur. J. Biochem. 55: 573-585.
    • (1975) Eur. J. Biochem. , vol.55 , pp. 573-585
    • Portier, C.1
  • 42
    • 0027945686 scopus 로고
    • A protein complex mediating mRNA degradation in Escherichia coli
    • Py, B., H. Causton, E.A. Mudd, and C.F. Higgins. 1994. A protein complex mediating mRNA degradation 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
  • 43
    • 0029922992 scopus 로고    scopus 로고
    • A DEAD-box RNA helicase in the Escherichia coli RNA degradosome
    • Py, B., C.F. Higgins, H.M. Krisch, 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    Krisch, H.M.3    Carpousis, A.J.4
  • 44
    • 0029827261 scopus 로고    scopus 로고
    • Bacterial poly(A) polymerase: An enzyme that modulates RNA stability
    • Raynal, L.C., H.M. Krisch, and A.J. Carpousis. 1996. Bacterial poly(A) polymerase: An enzyme that modulates RNA stability. Biochimie 78: 390-398.
    • (1996) Biochimie , vol.78 , pp. 390-398
    • Raynal, L.C.1    Krisch, H.M.2    Carpousis, A.J.3
  • 45
    • 0025176473 scopus 로고
    • Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4B
    • Rozen, F., I. Edery, K. Meerovitch, T.E. Dever, W.C. Merrick, and N. Sonenberg. 1990. Bidirectional RNA helicase activity of eucaryotic translation initiation factors 4A and 4B. Mol. Cell. Biol. 10: 1134-1144.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1134-1144
    • Rozen, F.1    Edery, I.2    Meerovitch, K.3    Dever, T.E.4    Merrick, W.C.5    Sonenberg, N.6
  • 47
    • 0026569419 scopus 로고
    • D-E-A-D protein family of putative RNA helicase
    • Schmid, S.R. and P. Linder. 1992. D-E-A-D protein family of putative RNA helicase. Mol. Microbiol. 6: 283-292.
    • (1992) Mol. Microbiol. , vol.6 , pp. 283-292
    • Schmid, S.R.1    Linder, P.2
  • 48
    • 0031944934 scopus 로고    scopus 로고
    • Specific RecA amino acid changes affect RecA-UmuD'C interaction
    • Sommer, S. , F. Boudsocq, R. Devoret, and A. Bailone. 1998. Specific RecA amino acid changes affect RecA-UmuD'C interaction. Mol. Microbiol. 28: 281-292.
    • (1998) Mol. Microbiol. , vol.28 , pp. 281-292
    • Sommer, S.1    Boudsocq, F.2    Devoret, R.3    Bailone, A.4
  • 49
    • 0017648969 scopus 로고
    • Purification and characterization of polynucleotide phosphorylase from Escherichia coli
    • Soreq, H. and U.Z. Littauer. 1977. Purification and characterization of polynucleotide phosphorylase from Escherichia coli. J. Biol. Chem. 252: 6885-6888.
    • (1977) J. Biol. Chem. , vol.252 , pp. 6885-6888
    • Soreq, H.1    Littauer, U.Z.2
  • 50
    • 0015240433 scopus 로고
    • The purification and characterization of Escherichia coli enolase
    • Spring, T.G. and F. Wold. 1971. The purification and characterization of Escherichia coli enolase. J. Biol. Chem. 246: 6797-6802.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6797-6802
    • Spring, T.G.1    Wold, F.2
  • 51
    • 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
  • 52
    • 0028945837 scopus 로고
    • RNA degradation in Escherichia coli regulated by 3′ adenylation and 5′ phosphorylation
    • Xu, F. and S.N. Cohen. 1995. RNA degradation in Escherichia coli 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.