메뉴 건너뛰기




Volumn 184, Issue 22, 2002, Pages 6250-6259

Bacillus subtilis YhaM, a member of a new family of 3′-to-5′ exonucleases in gram-positive bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; EXONUCLEASE; POLYRIBONUCLEOTIDE NUCLEOTIDYLTRANSFERASE; PROTEIN YHAM; RIBONUCLEASE; UNCLASSIFIED DRUG;

EID: 0036842854     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.22.6250-6259.2002     Document Type: Article
Times cited : (53)

References (53)
  • 1
    • 0028031195 scopus 로고
    • Identification of an activity that interacts with the 3′ untranslated region of c-myc RNA and the role of its target sequence in mediating rapid mRNA degradation
    • Alberta, J. A., K. Rundell, and C. D. Stiles. 1994. Identification of an activity that interacts with the 3′ untranslated region of c-myc RNA and the role of its target sequence in mediating rapid mRNA degradation. J. Biol. Chem. 269:4532-4538.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4532-4538
    • Alberta, J.A.1    Rundell, K.2    Stiles, C.D.3
  • 4
    • 0032408864 scopus 로고    scopus 로고
    • The HD domain defines a new superfamily of metal-dependent phosphohydrolases
    • Aravind, L., and E. V. Koonin. 1998, The HD domain defines a new superfamily of metal-dependent phosphohydrolases. Trends Biochem. Sci. 23:469-472.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 469-472
    • Aravind, L.1    Koonin, E.V.2
  • 5
    • 0034814879 scopus 로고    scopus 로고
    • A natural classification of ribonucleases
    • Aravind, L., and E. V. Koonin. 2001. A natural classification of ribonucleases. Methods Enzymol. 341:3-28.
    • (2001) Methods Enzymol. , vol.341 , pp. 3-28
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 0027391014 scopus 로고
    • Analysis of mRNA decay and rRNA processing in Escherichia coli multiple mutants carrying a deletion in RNase III
    • Babitzke, P., L. Granger, J. Olszewslo, and S. R. Kushner. 1993. Analysis of mRNA decay and rRNA processing in Escherichia coli multiple mutants carrying a deletion in RNase III. J. Bacteriol. 175:229-239.
    • (1993) J. Bacteriol. , vol.175 , pp. 229-239
    • Babitzke, P.1    Granger, L.2    Olszewslo, J.3    Kushner, S.R.4
  • 7
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch, A., and R, Apweiler. 2000. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 28:45-48.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 9
    • 0031734294 scopus 로고    scopus 로고
    • Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis
    • Bechhofer, D. H., and W. Wang. 1998. Decay of ermC mRNA in a polynucleotide phosphorylase mutant of Bacillus subtilis. J. Bacteriol. 180:5968-5977.
    • (1998) J. Bacteriol. , vol.180 , pp. 5968-5977
    • Bechhofer, D.H.1    Wang, W.2
  • 10
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • Bochkarev, A., R. A. Pfuetzner, A. M. Edwards, and L. Frappier. 1997. Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA. Nature 385:176-181.
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 11
    • 0033575671 scopus 로고    scopus 로고
    • The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding
    • Bochkarev, A., E. Bochkareva, L. Frappier, and A. M. Edwards. 1999. The crystal structure of the complex of replication protein A subunits RPA32 and RPA14 reveals a mechanism for single-stranded DNA binding. EMBO J. 18:4498-4504.
    • (1999) EMBO J. , vol.18 , pp. 4498-4504
    • Bochkarev, A.1    Bochkareva, E.2    Frappier, L.3    Edwards, A.M.4
  • 12
    • 0033559269 scopus 로고    scopus 로고
    • Massive presence of the Escherichia coli "major cold-shock protein" CspA under non-stress conditions
    • Brandi, A., R. Spurio, C. O. Gualerzi, and C. L. Pon. 1999. Massive presence of the Escherichia coli "major cold-shock protein" CspA under non-stress conditions. EMBO J. 18:1653-1659.
    • (1999) EMBO J. , vol.18 , pp. 1653-1659
    • Brandi, A.1    Spurio, R.2    Gualerzi, C.O.3    Pon, C.L.4
  • 13
    • 0027014332 scopus 로고
    • Compilation of superlinker vectors
    • Brosius, J. 1992. Compilation of superlinker vectors. Methods Enzymol. 216:469-483.
    • (1992) Methods Enzymol. , vol.216 , pp. 469-483
    • Brosius, J.1
  • 14
    • 0031471204 scopus 로고    scopus 로고
    • The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold
    • Bycroft, M., T. J. Hubbard, M. Proctor, S. M. Freund, and A. G. Murzin. 1997. The solution structure of the S1 RNA binding domain: A member of an ancient nucleic acid-binding fold. Cell 88:235-242.
    • (1997) Cell , vol.88 , pp. 235-242
    • Bycroft, M.1    Hubbard, T.J.2    Proctor, M.3    Freund, S.M.4    Murzin, A.G.5
  • 15
    • 0033972084 scopus 로고    scopus 로고
    • Purification and characterization of the tRNA-processing enzyme RNase BN
    • Callahan, C., D. Neri-Cortes, and M. P. Deutscher. 2000. Purification and characterization of the tRNA-processing enzyme RNase BN. J. Biol. Chem. 275:1030-1034.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1030-1034
    • Callahan, C.1    Neri-Cortes, D.2    Deutscher, M.P.3
  • 16
    • 0032486392 scopus 로고    scopus 로고
    • The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R
    • Cheng, Z.-F., Y. Zuo, Z. Li, K. E. Rudd, and M. P. Deutscher. 1998. The vacB gene required for virulence in Shigella flexneri and Escherichia coli encodes the exoribonuclease RNase R. J. Biol. Chem. 273:14077-14080.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14077-14080
    • Cheng, Z.-F.1    Zuo, Y.2    Li, Z.3    Rudd, K.E.4    Deutscher, M.P.5
  • 17
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • Coburn, G. A., and G. A. Mackie. 1999. Degradation of mRNA in Escherichia coli: An old problem with some new twists. Prog. Nucleic Acid Res. Mol. Biol. 62:55-108.
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.62 , pp. 55-108
    • Coburn, G.A.1    Mackie, G.A.2
  • 18
    • 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
  • 19
    • 0028875887 scopus 로고
    • Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys)
    • Commans, S., P. Plateau, S. Blanquet, and F. Dardel. 1995. Solution structure of the anticodon-binding domain of Escherichia coli lysyl-tRNA synthetase and studies of its interaction with tRNA(Lys). J. Mol. Biol. 253:100-113.
    • (1995) J. Mol. Biol. , vol.253 , pp. 100-113
    • Commans, S.1    Plateau, P.2    Blanquet, S.3    Dardel, F.4
  • 20
    • 0031547969 scopus 로고    scopus 로고
    • Processing of the Bacillus subtilis thrS leader mRNA is RNase E-dependent in Escherichia coli
    • Condon, C., H. Putzer, D, Luo, and M. Grunberg-Manago. 1997. Processing of the Bacillus subtilis thrS leader mRNA is RNase E-dependent in Escherichia coli. J. Mol. Biol. 268:235-242.
    • (1997) J. Mol. Biol. , vol.268 , pp. 235-242
    • Condon, C.1    Putzer, H.2    Luo, D.3    Grunberg-Manago, M.4
  • 21
    • 0035257090 scopus 로고    scopus 로고
    • Identification of the gene encoding the 5S ribosomal RNA maturase in Bacillus subtilis: Mature 5S rRNA is dispensable for ribosome function
    • Condon, C., D. Brechemier-Baey, B. Beltchev, M. Grunberg-Manago, and H. Putzer. 2001. Identification of the gene encoding the 5S ribosomal RNA maturase in Bacillus subtilis: Mature 5S rRNA is dispensable for ribosome function. RNA 7:242-253.
    • (2001) RNA , vol.7 , pp. 242-253
    • Condon, C.1    Brechemier-Baey, D.2    Beltchev, B.3    Grunberg-Manago, M.4    Putzer, H.5
  • 22
    • 0026334860 scopus 로고
    • Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis
    • Deutscher, M. P., and N. B. Reuven. 1991. Enzymatic basis for hydrolytic versus phosphorolytic mRNA degradation in Escherichia coli and Bacillus subtilis. Proc. Natl. Acad. Sci. USA 88:3277-3280.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3277-3280
    • Deutscher, M.P.1    Reuven, N.B.2
  • 23
    • 0003395950 scopus 로고
    • Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12
    • Donovan, W. P., and S. R. Kushner. 1986. Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 83:120-124.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 120-124
    • Donovan, W.P.1    Kushner, S.R.2
  • 24
    • 0015222721 scopus 로고
    • Fate of transforming DNA following uptake by competent Bacillus subtilis. I. Formation and properties of the donor-recipient complex
    • Dubnau, D., and R. Davidoff-Abelson. 1971. Fate of transforming DNA following uptake by competent Bacillus subtilis. I. Formation and properties of the donor-recipient complex. J. Mol. Biol. 56:209-221.
    • (1971) J. Mol. Biol. , vol.56 , pp. 209-221
    • Dubnau, D.1    Davidoff-Abelson, R.2
  • 25
    • 0031743421 scopus 로고    scopus 로고
    • Profile hidden Markov models
    • Eddy, S. R. 1998. Profile hidden Markov models. Bioinformatics 14:755-763.
    • (1998) Bioinformatics , vol.14 , pp. 755-763
    • Eddy, S.R.1
  • 26
    • 0022535021 scopus 로고
    • cmp, a cis-acting plasmid locus that increases interaction between replication origin and initiator protein
    • Gennaro, M. L., and R. P. Novick. 1986. cmp, a cis-acting plasmid locus that increases interaction between replication origin and initiator protein. J. Bacteriol. 168:160-166.
    • (1986) J. Bacteriol. , vol.168 , pp. 160-166
    • Gennaro, M.L.1    Novick, R.P.2
  • 27
    • 0033551137 scopus 로고    scopus 로고
    • Oligoribonuclease is an essential component of the mRNA decay pathway
    • Ghosh, S., and M. P. Deutscher. 1999. Oligoribonuclease is an essential component of the mRNA decay pathway. Proc. Natl. Acad. Sci. USA 96:4372-4377.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4372-4377
    • Ghosh, S.1    Deutscher, M.P.2
  • 29
    • 0025295967 scopus 로고
    • Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants
    • Grant, S. G. N., J. Jessee, F. R. Bloom, and D. Hanahan. 1990. Differential plasmid rescue from transgenic mouse DNAs into Escherichia coli methylation-restriction mutants. Proc. Natl. Acad. Sci. USA 87:4645-4649.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4645-4649
    • Grant, S.G.N.1    Jessee, J.2    Bloom, F.R.3    Hanahan, D.4
  • 30
    • 0034533785 scopus 로고    scopus 로고
    • Endoribonuclease RNase III is essential in Bacillus subtilis
    • Herskovitz, M. A., and D. H. Bechhofer, 2000. Endoribonuclease RNase III is essential in Bacillus subtilis. Mol. Microbiol. 38:1027-1033.
    • (2000) Mol. Microbiol. , vol.38 , pp. 1027-1033
    • Herskovitz, M.A.1    Bechhofer, D.H.2
  • 31
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones, P. G., R. A. VanBogelen, and F. C. Neidhardt. 1987. Induction of proteins in response to low temperature in Escherichia coli. J. Bacteriol. 169:2092-2095.
    • (1987) J. Bacteriol. , vol.169 , pp. 2092-2095
    • Jones, P.G.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 32
    • 0032845822 scopus 로고    scopus 로고
    • Regulation of the expression of the cold shock proteins CspB and CspC in Bacillus subtilis
    • Kaan, T., B. Jurgen, and T. Schweder. 1999. Regulation of the expression of the cold shock proteins CspB and CspC in Bacillus subtilis. Mol. Gen. Genet. 262:351-354.
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 351-354
    • Kaan, T.1    Jurgen, B.2    Schweder, T.3
  • 33
    • 0017078591 scopus 로고
    • Isolation and properties of a cyclic guanosine-monophosphate sensitive intracellular ribonuclease from Bacillus subtilis
    • Kerjan, P., and J. Szulmaster, 1976. Isolation and properties of a cyclic guanosine-monophosphate sensitive intracellular ribonuclease from Bacillus subtilis. Biochimie 58:533-541.
    • (1976) Biochimie , vol.58 , pp. 533-541
    • Kerjan, P.1    Szulmaster, J.2
  • 35
    • 0030047027 scopus 로고    scopus 로고
    • Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis
    • Luttinger, A., J. Hahn, and D. Dubnau. 1996. Polynucleotide phosphorylase is necessary for competence development in Bacillus subtilis. Mol. Microbiol. 19:343-356.
    • (1996) Mol. Microbiol. , vol.19 , pp. 343-356
    • Luttinger, A.1    Hahn, J.2    Dubnau, D.3
  • 36
    • 0027361297 scopus 로고
    • Identification of an intracellular pyrimidine-specific endoribonuclease from Bacillus subtilis
    • Mathur, S., V. J. Cannistraro, and D. Kennell. 1993. Identification of an intracellular pyrimidine-specific endoribonuclease from Bacillus subtilis. J. Bacteriol. 175:6717-6720.
    • (1993) J. Bacteriol. , vol.175 , pp. 6717-6720
    • Mathur, S.1    Cannistraro, V.J.2    Kennell, D.3
  • 37
    • 0029094248 scopus 로고
    • Recruiting proteins to the RNA world
    • Mattaj, I. W., and K. Nagai. 1995. Recruiting proteins to the RNA world. Nat. Struct. Biol. 2:518-522.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 518-522
    • Mattaj, I.W.1    Nagai, K.2
  • 38
    • 0027479161 scopus 로고
    • OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences
    • Murzin, A. G. 1993. OB (oligonucleotide/oligosaccharide binding)-fold: Common structural and functional solution for non-homologous sequences. EMBO J. 12:861-867.
    • (1993) EMBO J. , vol.12 , pp. 861-867
    • Murzin, A.G.1
  • 40
    • 0033995502 scopus 로고    scopus 로고
    • The yvaJ gene of Bacillus subtilis encodes a 3′-to-5′ exoribonuclease and is not essential in a strain lacking polynucleotide phosphorylase
    • Oussenko, I. A., and D. H. Bechhofer. 2000. The yvaJ gene of Bacillus subtilis encodes a 3′-to-5′ exoribonuclease and is not essential in a strain lacking polynucleotide phosphorylase. J. Bacteriol. 182:2639-2642.
    • (2000) J. Bacteriol. , vol.182 , pp. 2639-2642
    • Oussenko, I.A.1    Bechhofer, D.H.2
  • 41
    • 0242400018 scopus 로고    scopus 로고
    • Degradation of mRNA in bacteria: Emergence of ubiquitous features
    • Regnier, P., and C. M. Arraiano. 2000. Degradation of mRNA in bacteria: Emergence of ubiquitous features. Bioessays 22:235-244.
    • (2000) Bioessays , vol.22 , pp. 235-244
    • Regnier, P.1    Arraiano, C.M.2
  • 42
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali, A., and T. L. Blundell. 1993. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234:779-815.
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 43
    • 0032506030 scopus 로고    scopus 로고
    • Large-scale protein structure modeling of the Saccharomyces cerevisiae genome
    • Sanchez, R., and A. Sali. 1998. Large-scale protein structure modeling of the Saccharomyces cerevisiae genome. Proc. Natl. Acad. Sci. USA 95:13597-13602.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13597-13602
    • Sanchez, R.1    Sali, A.2
  • 44
    • 0023112742 scopus 로고
    • Plasmid-determined bleomycin resistance in Staphylococcus aureus
    • Semon, D., N. Rao Movva, T. F. Smith, M. El Alama, and J. Davies. 1987. Plasmid-determined bleomycin resistance in Staphylococcus aureus. Plasmid 17:46-53.
    • (1987) Plasmid , vol.17 , pp. 46-53
    • Semon, D.1    Rao Movva, N.2    Smith, T.F.3    El Alama, M.4    Davies, J.5
  • 45
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl, M. J. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins 17:355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 46
    • 0024672741 scopus 로고
    • Genetic analysis of the rnc operon of Escherichia coli
    • Takiff, H. E., S. Chen, and D. L. Court. 1989. Genetic analysis of the rnc operon of Escherichia coli. J. Bacteriol. 171:2581-2590.
    • (1989) J. Bacteriol. , vol.171 , pp. 2581-2590
    • Takiff, H.E.1    Chen, S.2    Court, D.L.3
  • 47
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 48
    • 0030002447 scopus 로고    scopus 로고
    • Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain
    • Wang, W., and D. H. Bechhofer. 1996. Properties of a Bacillus subtilis polynucleotide phosphorylase deletion strain. J. Bacteriol. 178:2375-2382.
    • (1996) J. Bacteriol. , vol.178 , pp. 2375-2382
    • Wang, W.1    Bechhofer, D.H.2
  • 49
    • 0035050516 scopus 로고    scopus 로고
    • Induction of CspA, an E. coli major cold-shock protein, upon nutritional upshift at 37°C
    • Yamanaka, K., and M. Inouye. 2001. Induction of CspA, an E. coli major cold-shock protein, upon nutritional upshift at 37°C. Genes Cells 6:279-290.
    • (2001) Genes Cells , vol.6 , pp. 279-290
    • Yamanaka, K.1    Inouye, M.2
  • 50
    • 0035046480 scopus 로고    scopus 로고
    • Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coli
    • Yamanaka, K., and M. Inouye. 2001. Selective mRNA degradation by polynucleotide phosphorylase in cold shock adaptation in Escherichia coli. J. Bacteriol. 183:2808-2816.
    • (2001) J. Bacteriol. , vol.183 , pp. 2808-2816
    • Yamanaka, K.1    Inouye, M.2
  • 51
    • 0031939953 scopus 로고    scopus 로고
    • Polyribonucleotide phosphorylase is a double-stranded DNA-binding protein
    • Zhang, P., J.-L. Vigne, and S. H. Mellon. 1998. Polyribonucleotide phosphorylase is a double-stranded DNA-binding protein. DNA Cell Biol. 17:169-175.
    • (1998) DNA Cell Biol. , vol.17 , pp. 169-175
    • Zhang, P.1    Vigne, J.-L.2    Mellon, S.H.3
  • 52
    • 0031025142 scopus 로고    scopus 로고
    • Binding of a novel host factor to the pT181 plasmid replication enhancer
    • Zhang, Q., S. Soares de Oliveira, R. Colangell, and M. L. Gennaro. 1997. Binding of a novel host factor to the pT181 plasmid replication enhancer. J. Bacteriol. 179:684-688.
    • (1997) J. Bacteriol. , vol.179 , pp. 684-688
    • Zhang, Q.1    Soares de Oliveira, S.2    Colangell, R.3    Gennaro, M.L.4
  • 53
    • 0035283033 scopus 로고    scopus 로고
    • Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution
    • Zuo, Y., and M. P. Deutscher. 2001. Exoribonuclease superfamilies: Structural analysis and phylogenetic distribution. Nucleic Acids Res. 29:1017-1026.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1017-1026
    • Zuo, Y.1    Deutscher, M.P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.