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Volumn 327, Issue 2, 2005, Pages 382-392

Characterization of Aquifex aeolicus RNase E/G

Author keywords

Aquifex aeolicus; RNA processing; Thermophilic RNase

Indexed keywords

BACTERIAL ENZYME; NUCLEASE; OLIGONUCLEOTIDE; RIBONUCLEASE; RIBONUCLEASE E; RIBONUCLEASE G; RNA; RNA PRECURSOR; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 11144297942     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.12.017     Document Type: Article
Times cited : (20)

References (52)
  • 1
    • 0031000662 scopus 로고    scopus 로고
    • RNase E: Still a wonderfully mysterious enzyme
    • S.N. Cohen, and K.J. McDowall RNase E: still a wonderfully mysterious enzyme Mol. Microbiol. 23 1997 1099 1106
    • (1997) Mol. Microbiol. , vol.23 , pp. 1099-1106
    • Cohen, S.N.1    McDowall, K.J.2
  • 2
    • 0033368475 scopus 로고    scopus 로고
    • Messenger RNA stability and its role in control of gene expression in bacteria and phages
    • M. Grunberg-Manago Messenger RNA stability and its role in control of gene expression in bacteria and phages Annu. Rev. Genet. 33 1999 193 227
    • (1999) Annu. Rev. Genet. , vol.33 , pp. 193-227
    • Grunberg-Manago, M.1
  • 3
    • 0032617132 scopus 로고    scopus 로고
    • Degradation of mRNA in Escherichia coli: An old problem with some new twists
    • G.A. Coburn, and G.A. Mackie Degradation of mRNA in Escherichia coli: an old problem with some new twists Prog. Nucleic Acid Res. Mol. Biol. 62 1999 55 108
    • (1999) Prog. Nucleic Acid Res. Mol. Biol. , vol.62 , pp. 55-108
    • Coburn, G.A.1    MacKie, G.A.2
  • 4
    • 0027955358 scopus 로고
    • Cytoplasmic axial filaments in Escherichia coli cells: Possible function in the mechanism of chromosome segregation and cell division
    • Y. Okada, M. Wachi, A. Hirata, K. Suzuki, K. Nagai, and M. Matsuhashi Cytoplasmic axial filaments in Escherichia coli cells: possible function in the mechanism of chromosome segregation and cell division J. Bacteriol. 176 1994 917 922
    • (1994) J. Bacteriol. , vol.176 , pp. 917-922
    • Okada, Y.1    Wachi, M.2    Hirata, A.3    Suzuki, K.4    Nagai, K.5    Matsuhashi, M.6
  • 5
    • 0027903598 scopus 로고
    • Possible function of the cytoplasmic axial filaments in chromosomal segregation and cellular division of Escherichia coli
    • Y. Okada, T. Shibata, and M. Matsuhashi Possible function of the cytoplasmic axial filaments in chromosomal segregation and cellular division of Escherichia coli Sci. Prog. 77 Pt 3-4 1993 253 264
    • (1993) Sci. Prog. , vol.77 , Issue.34 , pp. 253-264
    • Okada, Y.1    Shibata, T.2    Matsuhashi, M.3
  • 6
    • 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
    • K.J. McDowall, R.G. Hernandez, S. Lin-Chao, and S.N. Cohen 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 1993 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
  • 7
    • 0033532514 scopus 로고    scopus 로고
    • Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA
    • M. Wachi, G. Umitsuki, M. Shimizu, A. Takada, and K. Nagai Escherichia coli cafA gene encodes a novel RNase, designated as RNase G, involved in processing of the 5′ end of 16S rRNA Biochem. Biophys. Res. Commun. 259 1999 483 488
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 483-488
    • Wachi, M.1    Umitsuki, G.2    Shimizu, M.3    Takada, A.4    Nagai, K.5
  • 8
    • 0033577789 scopus 로고    scopus 로고
    • RNase G (CafA protein) and RNase e are both required for the 5′ maturation of 16S ribosomal RNA
    • Z. Li, S. Pandit, and M.P. Deutscher RNase G (CafA protein) and RNase E are both required for the 5′ maturation of 16S ribosomal RNA EMBO J. 18 1999 2878 2885
    • (1999) EMBO J. , vol.18 , pp. 2878-2885
    • Li, Z.1    Pandit, S.2    Deutscher, M.P.3
  • 9
    • 0034708447 scopus 로고    scopus 로고
    • The CafA protein required for the 5′-maturation of 16 S rRNA is a 5′- end-dependent ribonuclease that has context-dependent broad sequence specificity
    • M.R. Tock, A.P. Walsh, G. Carroll, and K.J. McDowall The CafA protein required for the 5′-maturation of 16 S rRNA is a 5′- end-dependent ribonuclease that has context-dependent broad sequence specificity J. Biol. Chem. 275 2000 8726 8732
    • (2000) J. Biol. Chem. , vol.275 , pp. 8726-8732
    • Tock, M.R.1    Walsh, A.P.2    Carroll, G.3    McDowall, K.J.4
  • 10
    • 0034005317 scopus 로고    scopus 로고
    • Regions of RNase e important for 5′-end-dependent RNA cleavage and autoregulated synthesis
    • X. Jiang, A. Diwa, and J.G. Belasco Regions of RNase E important for 5′-end-dependent RNA cleavage and autoregulated synthesis J. Bacteriol. 182 2000 2468 2475
    • (2000) J. Bacteriol. , vol.182 , pp. 2468-2475
    • Jiang, X.1    Diwa, A.2    Belasco, J.G.3
  • 11
    • 0032531768 scopus 로고    scopus 로고
    • Ribonuclease e is a 5′-end-dependent endonuclease
    • G.A. Mackie Ribonuclease E is a 5′-end-dependent endonuclease Nature 395 1998 720 723
    • (1998) Nature , vol.395 , pp. 720-723
    • MacKie, G.A.1
  • 12
    • 0002494745 scopus 로고
    • RNA Processing and Degradation by RNase K and RNase e
    • J. Belasco G. Brawerman Academic Press San Diego
    • O. Melefors, U. Lundberg, and A. von Gabain RNA Processing and Degradation by RNase K and RNase E J. Belasco G. Brawerman Control of Messenger RNA Stability 1993 Academic Press San Diego 53 70
    • (1993) Control of Messenger RNA Stability , pp. 53-70
    • Melefors, O.1    Lundberg, U.2    Von Gabain, A.3
  • 13
    • 0018582283 scopus 로고
    • RNase E, an RNA processing enzyme from Escherichia coli
    • T.K. Misra, and D. Apirion RNase E, an RNA processing enzyme from Escherichia coli J. Biol. Chem. 254 1979 11154 11159
    • (1979) J. Biol. Chem. , vol.254 , pp. 11154-11159
    • Misra, T.K.1    Apirion, D.2
  • 14
    • 0036210631 scopus 로고    scopus 로고
    • RNase e plays an essential role in the maturation of Escherichia coli tRNA precursors
    • Z. Li, and M.P. Deutscher RNase E plays an essential role in the maturation of Escherichia coli tRNA precursors RNA 8 2002 97 109
    • (2002) RNA , vol.8 , pp. 97-109
    • Li, Z.1    Deutscher, M.P.2
  • 15
    • 0037048524 scopus 로고    scopus 로고
    • 3′-end processing of precursor M1 RNA by the N-terminal half of RNase e
    • S. Sim, K.S. Kim, and Y. Lee 3′-end processing of precursor M1 RNA by the N-terminal half of RNase E FEBS Lett. 529 2002 225 231
    • (2002) FEBS Lett. , vol.529 , pp. 225-231
    • Sim, S.1    Kim, K.S.2    Lee, Y.3
  • 16
    • 0033607239 scopus 로고    scopus 로고
    • RNase e is required for the maturation of ssrA RNA and normal ssrA RNA peptide-tagging activity
    • S. Lin-Chao, C.L. Wei, and Y.T. Lin RNase E is required for the maturation of ssrA RNA and normal ssrA RNA peptide-tagging activity Proc. Natl. Acad. Sci. USA 96 1999 12406 12411
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12406-12411
    • Lin-Chao, S.1    Wei, C.L.2    Lin, Y.T.3
  • 17
    • 0036308316 scopus 로고    scopus 로고
    • Extensive overproduction of the AdhE protein by rng mutations depends on mutations in the cra gene or in the Cra-box of the adhE promoter
    • N. Kaga, G. Umitsuki, D.P. Clark, K. Nagai, and M. Wachi Extensive overproduction of the AdhE protein by rng mutations depends on mutations in the cra gene or in the Cra-box of the adhE promoter Biochem. Biophys. Res. Commun. 295 2002 92 97
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 92-97
    • Kaga, N.1    Umitsuki, G.2    Clark, D.P.3    Nagai, K.4    Wachi, M.5
  • 18
    • 0036274640 scopus 로고    scopus 로고
    • RNase G complementation of rne null mutation identifies functional interrelationships with RNase e in Escherichia coli
    • K. Lee, J.A. Bernstein, and S.N. Cohen RNase G complementation of rne null mutation identifies functional interrelationships with RNase E in Escherichia coli Mol. Microbiol. 43 2002 1445 1456
    • (2002) Mol. Microbiol. , vol.43 , pp. 1445-1456
    • Lee, K.1    Bernstein, J.A.2    Cohen, S.N.3
  • 19
    • 0042497078 scopus 로고    scopus 로고
    • RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme enolase in Escherichia coli
    • N. Kaga, G. Umitsuki, K. Nagai, and M. Wachi RNase G-dependent degradation of the eno mRNA encoding a glycolysis enzyme enolase in Escherichia coli Biosci. Biotechnol. Biochem. 66 2002 2216 2220
    • (2002) Biosci. Biotechnol. Biochem. , vol.66 , pp. 2216-2220
    • Kaga, N.1    Umitsuki, G.2    Nagai, K.3    Wachi, M.4
  • 20
    • 0042665928 scopus 로고    scopus 로고
    • RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase e
    • M.C. Ow, T. Perwez, and S.R. Kushner RNase G of Escherichia coli exhibits only limited functional overlap with its essential homologue, RNase E Mol. Microbiol. 49 2003 607 622
    • (2003) Mol. Microbiol. , vol.49 , pp. 607-622
    • Ow, M.C.1    Perwez, T.2    Kushner, S.R.3
  • 21
    • 0036549769 scopus 로고    scopus 로고
    • The Escherichia coli RNA degradosome: Structure, function and relationship in other ribonucleolytic multienzyme complexes
    • A.J. Carpousis The Escherichia coli RNA degradosome: structure, function and relationship in other ribonucleolytic multienzyme complexes Biochem. Soc. Trans. 30 2002 150 155
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 150-155
    • Carpousis, A.J.1
  • 22
    • 0037115876 scopus 로고    scopus 로고
    • The phylogenetic distribution of bacterial ribonucleases
    • C. Condon, and H. Putzer The phylogenetic distribution of bacterial ribonucleases Nucleic Acids Res. 30 2002 5339 5346
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5339-5346
    • Condon, C.1    Putzer, H.2
  • 23
    • 0038687705 scopus 로고    scopus 로고
    • A Streptomyces coelicolor functional orthologue of Escherichia coli RNase e shows shuffling of catalytic and PNPase-binding domains
    • K. Lee, and S.N. Cohen A Streptomyces coelicolor functional orthologue of Escherichia coli RNase E shows shuffling of catalytic and PNPase-binding domains Mol. Microbiol. 48 2003 349 360
    • (2003) Mol. Microbiol. , vol.48 , pp. 349-360
    • Lee, K.1    Cohen, S.N.2
  • 24
    • 11144263283 scopus 로고    scopus 로고
    • R. Huber, K.O. Stetter, in: London: Nature Publishing Group, 1999
    • R. Huber, K.O. Stetter, in: London: Nature Publishing Group, 1999
  • 25
    • 0027389009 scopus 로고
    • Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli
    • B. Sohlberg, U. Lundberg, F.U. Hartl, and A. von Gabain Functional interaction of heat shock protein GroEL with an RNase E-like activity in Escherichia coli Proc. Natl. Acad. Sci. USA 90 1993 277 281
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 277-281
    • Sohlberg, B.1    Lundberg, U.2    Hartl, F.U.3    Von Gabain, A.4
  • 26
    • 0028987956 scopus 로고
    • Site-specific RNase e cleavage of oligonucleotides and inhibition by stem-loops
    • K.J. McDowall, V.R. Kaberdin, S.W. Wu, S.N. Cohen, and S. Lin-Chao Site-specific RNase E cleavage of oligonucleotides and inhibition by stem-loops Nature 374 1995 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
  • 27
    • 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
    • K.J. McDowall, and S.N. Cohen 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 1996 349 355
    • (1996) J. Mol. Biol. , vol.255 , pp. 349-355
    • McDowall, K.J.1    Cohen, S.N.2
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0242666860 scopus 로고    scopus 로고
    • Determination of the catalytic parameters of the N-terminal half of E. coli ribonuclease e and the identification of critical functional groups in RNA substrates
    • Y. Redko, M.R. Tock, C.J. Adams, V.R. Kaberdin, J.A. Grasby, and K.J. McDowall Determination of the catalytic parameters of the N-terminal half of E. coli ribonuclease E and the identification of critical functional groups in RNA substrates J. Biol. Chem. 278 2003 44001 44008
    • (2003) J. Biol. Chem. , vol.278 , pp. 44001-44008
    • Redko, Y.1    Tock, M.R.2    Adams, C.J.3    Kaberdin, V.R.4    Grasby, J.A.5    McDowall, K.J.6
  • 30
    • 0025814610 scopus 로고
    • The rate of processing and degradation of antisense RNAI regulates the replication of ColE1-type plasmids in vivo
    • S. Lin-Chao, and S.N. Cohen The rate of processing and degradation of antisense RNAI regulates the replication of ColE1-type plasmids in vivo Cell 65 1991 1233 1242
    • (1991) Cell , vol.65 , pp. 1233-1242
    • Lin-Chao, S.1    Cohen, S.N.2
  • 31
    • 0025731898 scopus 로고
    • Control of ColE1 plasmid replication by antisense RNA
    • G. Cesareni, C.M. Helmer, and L. Castagnoli Control of ColE1 plasmid replication by antisense RNA Trends Genet. 7 1991 230 235
    • (1991) Trends Genet. , vol.7 , pp. 230-235
    • Cesareni, G.1    Helmer, C.M.2    Castagnoli, L.3
  • 32
    • 15844404508 scopus 로고    scopus 로고
    • RNase e cleaves at multiple sites in bubble regions of RNA I stem loops yielding products that dissociate differentially from the enzyme
    • V.R. Kaberdin, Y.H. Chao, and S. Lin-Chao RNase E cleaves at multiple sites in bubble regions of RNA I stem loops yielding products that dissociate differentially from the enzyme J. Biol. Chem. 271 1996 13103 13109
    • (1996) J. Biol. Chem. , vol.271 , pp. 13103-13109
    • Kaberdin, V.R.1    Chao, Y.H.2    Lin-Chao, S.3
  • 33
    • 0018034154 scopus 로고
    • Structural analysis and in vitro processing to p5 rRNA of a 9S RNA molecule isolated from an rne mutant of E. coli
    • B.K. Ghora, and D. Apirion Structural analysis and in vitro processing to p5 rRNA of a 9S RNA molecule isolated from an rne mutant of E. coli Cell 15 1978 1055 1066
    • (1978) Cell , vol.15 , pp. 1055-1066
    • Ghora, B.K.1    Apirion, D.2
  • 34
    • 0027054379 scopus 로고
    • Structural requirements for the processing of Escherichia coli 5 S ribosomal RNA by RNase e in vitro
    • R.S. Cormack, and G.A. Mackie Structural requirements for the processing of Escherichia coli 5 S ribosomal RNA by RNase E in vitro J. Mol. Biol. 228 1992 1078 1090
    • (1992) J. Mol. Biol. , vol.228 , pp. 1078-1090
    • Cormack, R.S.1    MacKie, G.A.2
  • 35
    • 0037069357 scopus 로고    scopus 로고
    • The catalytic domain of RNase e shows inherent 3′ to 5′ directionality in cleavage site selection
    • Y. Feng, T.A. Vickers, and S.N. Cohen The catalytic domain of RNase E shows inherent 3′ to 5′ directionality in cleavage site selection Proc. Natl. Acad. Sci. USA 99 2002 14746 14751
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14746-14751
    • Feng, Y.1    Vickers, T.A.2    Cohen, S.N.3
  • 36
    • 0242395917 scopus 로고    scopus 로고
    • Probing the substrate specificity of Escherichia coli RNase e using a novel oligonucleotide-based assay
    • V.R. Kaberdin Probing the substrate specificity of Escherichia coli RNase E using a novel oligonucleotide-based assay Nucleic Acids Res. 31 2003 4710 4716
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4710-4716
    • Kaberdin, V.R.1
  • 39
    • 0037031594 scopus 로고    scopus 로고
    • An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes
    • J. Johansson, P. Mandin, A. Renzoni, C. Chiaruttini, M. Springer, and P. Cossart An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes Cell 110 2002 551 561
    • (2002) Cell , vol.110 , pp. 551-561
    • Johansson, J.1    Mandin, P.2    Renzoni, A.3    Chiaruttini, C.4    Springer, M.5    Cossart, P.6
  • 41
    • 0034717156 scopus 로고    scopus 로고
    • Stability and stabilization of globular proteins in solution
    • R. Jaenicke Stability and stabilization of globular proteins in solution J. Biotechnol. 79 2000 193 203
    • (2000) J. Biotechnol. , vol.79 , pp. 193-203
    • Jaenicke, R.1
  • 43
    • 4143138726 scopus 로고    scopus 로고
    • Structural characterization of the RNase e S1 domain and identification of its oligonucleotide-binding and dimerization interfaces
    • M. Schubert, R.E. Edge, P. Lario, M.A. Cook, N.C. Strynadka, G.A. Mackie, and L.P. McIntosh Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces J. Mol. Biol. 341 2004 37 54
    • (2004) J. Mol. Biol. , vol.341 , pp. 37-54
    • Schubert, M.1    Edge, R.E.2    Lario, P.3    Cook, M.A.4    Strynadka, N.C.5    MacKie, G.A.6    McIntosh, L.P.7
  • 44
    • 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
    • V.R. Kaberdin, A. Miczak, J.S. Jakobsen, S. Lin-Chao, K.J. McDowall, and A. von Gabain 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 1998 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
  • 45
    • 0030924592 scopus 로고    scopus 로고
    • A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease e of Escherichia coli
    • J.M. Hagege, and S.N. Cohen A developmentally regulated Streptomyces endoribonuclease resembles ribonuclease E of Escherichia coli Mol. Microbiol. 25 1997 1077 1090
    • (1997) Mol. Microbiol. , vol.25 , pp. 1077-1090
    • Hagege, J.M.1    Cohen, S.N.2
  • 46
    • 0022609327 scopus 로고
    • Local stability of DNA and RNA secondary structure and its relation to biological functions
    • A. Wada, and A. Suyama Local stability of DNA and RNA secondary structure and its relation to biological functions Prog. Biophys. Mol. Biol. 47 1986 113 157
    • (1986) Prog. Biophys. Mol. Biol. , vol.47 , pp. 113-157
    • Wada, A.1    Suyama, A.2
  • 47
    • 0035819839 scopus 로고    scopus 로고
    • High guanine-cytosine content is not an adaptation to high temperature: A comparative analysis amongst prokaryotes
    • L.D. Hurst, and A.R. Merchant High guanine-cytosine content is not an adaptation to high temperature: a comparative analysis amongst prokaryotes Proc. R. Soc. Lond. B Biol. Sci. 268 2001 493 497
    • (2001) Proc. R. Soc. Lond. B Biol. Sci. , vol.268 , pp. 493-497
    • Hurst, L.D.1    Merchant, A.R.2
  • 48
    • 0030900384 scopus 로고    scopus 로고
    • Relationships between genomic G+C content, RNA secondary structures, and optimal growth temperature in prokaryotes
    • N. Galtier, and J.R. Lobry Relationships between genomic G+C content, RNA secondary structures, and optimal growth temperature in prokaryotes J. Mol. Evol. 44 1997 632 636
    • (1997) J. Mol. Evol. , vol.44 , pp. 632-636
    • Galtier, N.1    Lobry, J.R.2
  • 49
    • 1642565815 scopus 로고    scopus 로고
    • The bacterial Sm-like protein Hfq: A key player in RNA transactions
    • P. Valentin-Hansen, M. Eriksen, and C. Udesen The bacterial Sm-like protein Hfq: a key player in RNA transactions Mol. Microbiol. 51 2004 1525 1533
    • (2004) Mol. Microbiol. , vol.51 , pp. 1525-1533
    • Valentin-Hansen, P.1    Eriksen, M.2    Udesen, C.3
  • 50
    • 0142240435 scopus 로고    scopus 로고
    • Coincident Hfq binding and RNase e cleavage sites on mRNA and small regulatory RNAs
    • I. Moll, T. Afonyushkin, O. Vytvytska, V.R. Kaberdin, and U. Blasi Coincident Hfq binding and RNase E cleavage sites on mRNA and small regulatory RNAs RNA 9 2003 1308 1314
    • (2003) RNA , vol.9 , pp. 1308-1314
    • Moll, I.1    Afonyushkin, T.2    Vytvytska, O.3    Kaberdin, V.R.4    Blasi, U.5
  • 51
    • 0242380623 scopus 로고    scopus 로고
    • Sm-like proteins in Eubacteria: The crystal structure of the Hfq protein from Escherichia coli
    • C. Sauter, J. Basquin, and D. Suck Sm-like proteins in Eubacteria: the crystal structure of the Hfq protein from Escherichia coli Nucleic Acids Res. 31 2003 4091 4098
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4091-4098
    • Sauter, C.1    Basquin, J.2    Suck, D.3
  • 52
    • 0037428440 scopus 로고    scopus 로고
    • Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya
    • S. Thore, C. Mayer, C. Sauter, S. Weeks, and D. Suck Crystal structures of the Pyrococcus abyssi Sm core and its complex with RNA. Common features of RNA binding in archaea and eukarya J. Biol. Chem. 278 2003 1239 1247
    • (2003) J. Biol. Chem. , vol.278 , pp. 1239-1247
    • Thore, S.1    Mayer, C.2    Sauter, C.3    Weeks, S.4    Suck, D.5


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