메뉴 건너뛰기




Volumn 261, Issue 2, 1996, Pages 231-238

A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase centre of 23 S rRNA

Author keywords

23 S rRNA; Drug resistant mutant; Peptidyl transferase; Post transcriptional modification; Sparsomycin

Indexed keywords

ANISOMYCIN; CHLORAMPHENICOL; PEPTIDYLTRANSFERASE; PUROMYCIN; RIBOSOME RNA; RNA 23S; SPARSOMYCIN; URIDINE;

EID: 0030590237     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0455     Document Type: Article
Times cited : (36)

References (43)
  • 1
    • 0028131689 scopus 로고
    • A spontaneous mutation in the single 23 S rRNA gene of the thermophilic archaeon Sulfolobus acidocaldarius conferring multiple drug resistance
    • Aagaard, C., Phan, H., Trevisanato, S. & Garrett, R. A. (1994). A spontaneous mutation in the single 23 S rRNA gene of the thermophilic archaeon Sulfolobus acidocaldarius conferring multiple drug resistance. J. Bacteriol. 176, 7744-7747.
    • (1994) J. Bacteriol. , vol.176 , pp. 7744-7747
    • Aagaard, C.1    Phan, H.2    Trevisanato, S.3    Garrett, R.A.4
  • 2
    • 0002124045 scopus 로고
    • Peptidyl transferase inhibitors: Structure-activity relationship analyses by chemical modification
    • (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), American Society for Microbiology, Washington DC
    • Ballesta, J. P. G. & Lázaro, E. (1990). Peptidyl transferase inhibitors: structure-activity relationship analyses by chemical modification. In The Ribosome: Structure, Function and Evolution (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), pp. 502-510, American Society for Microbiology, Washington DC.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 502-510
    • Ballesta, J.P.G.1    Lázaro, E.2
  • 3
    • 0016166350 scopus 로고
    • 3H]Anisomycin binding to eukaryotic ribosomes
    • 3H]Anisomycin binding to eukaryotic ribosomes. J. Mol. Biol. 84, 603-623.
    • (1974) J. Mol. Biol. , vol.84 , pp. 603-623
    • Barbacid, M.1    Vázquez, D.2
  • 4
    • 0027519205 scopus 로고
    • Clustering of modified nucleotides at the functional center of bacterial rRNA
    • Brimacombe, R., Mitchell, P., Osswald, M., Stade, K. & Bochkariov, D. (1993). Clustering of modified nucleotides at the functional center of bacterial rRNA. FASEB J. 7, 161-167.
    • (1993) FASEB J. , vol.7 , pp. 161-167
    • Brimacombe, R.1    Mitchell, P.2    Osswald, M.3    Stade, K.4    Bochkariov, D.5
  • 5
    • 0022036495 scopus 로고
    • Insensitivity of archaebacterial ribosomes to protein synthesis inhibitors. Evolutionary implications
    • Cammarano, P., Teichner, A., Londei, P., Acca, M., Nicolaus, B., Sanz, J. L. & Amils, R. (1985). Insensitivity of archaebacterial ribosomes to protein synthesis inhibitors. Evolutionary implications. EMBO J. 4, 811-816.
    • (1985) EMBO J. , vol.4 , pp. 811-816
    • Cammarano, P.1    Teichner, A.2    Londei, P.3    Acca, M.4    Nicolaus, B.5    Sanz, J.L.6    Amils, R.7
  • 6
    • 0001683908 scopus 로고
    • Analysis of rRNA structure: Experimental and theoretical considerations
    • (Spedding, G., ed.), Oxford University Press, Oxford
    • Christiansen, J., Egebjerg, J., Larsen, N. & Garrett, R. A. (1990). Analysis of rRNA structure: experimental and theoretical considerations. In Ribosomes and Protein Biosythesis: A Practical Approach (Spedding, G., ed.), pp. 229-252, Oxford University Press, Oxford.
    • (1990) Ribosomes and Protein Biosythesis: A Practical Approach , pp. 229-252
    • Christiansen, J.1    Egebjerg, J.2    Larsen, N.3    Garrett, R.A.4
  • 7
    • 0002331708 scopus 로고
    • Recognition sites for antibiotics within rRNA
    • (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), American Society for Microbiology, Washington DC
    • Cundliffe, E. (1990). Recognition sites for antibiotics within rRNA. In The Ribosome: Structure, Function and Evolution (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), pp. 479-490, American Society for Microbiology, Washington DC.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 479-490
    • Cundliffe, E.1
  • 9
    • 0002476512 scopus 로고
    • Structural map of 23 S rRNA
    • (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), American Society for Microbiology, Washington DC
    • Egebjerg, J., Larsen, N. & Garrett, R. A. (1990). Structural map of 23 S rRNA. In The Ribosome: Structure, Function and Evolution (Hill, W., Dahlberg, A., Garrett, R. A., Moore, P., Schlessinger, D. & Warner, J., eds), pp. 168-179, American Society for Microbiology, Washington DC.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 168-179
    • Egebjerg, J.1    Larsen, N.2    Garrett, R.A.3
  • 13
    • 0015121549 scopus 로고
    • Change in methylation of 16 S rRNA associated with mutation to kasugamycin resistance in E. coli
    • Helser, T. L., Davies, J. E. & Dahlberg, J. E. (1971). Change in methylation of 16 S rRNA associated with mutation to kasugamycin resistance in E. coli. Nature New Biol. 233, 12-14.
    • (1971) Nature New Biol. , vol.233 , pp. 12-14
    • Helser, T.L.1    Davies, J.E.2    Dahlberg, J.E.3
  • 14
    • 0018774960 scopus 로고
    • The number, physical organization and transcription of rRNA cistrons in the archaebacterium Halobacterium halobium
    • Hofman, J. D., Lau, R. H. & Doolittle, W. F. (1979). The number, physical organization and transcription of rRNA cistrons in the archaebacterium Halobacterium halobium. Nucl. Acids Res. 7, 1321-1333.
    • (1979) Nucl. Acids Res. , vol.7 , pp. 1321-1333
    • Hofman, J.D.1    Lau, R.H.2    Doolittle, W.F.3
  • 15
    • 0020518233 scopus 로고
    • Effect of codon shortening and the antibiotics viomycin and sparsomycin upon the behaviour of bound aatRNA. Decoding at the ribosomal A-site
    • Hornig, H., Woolley, P. & Lührmann, R. (1983). Effect of codon shortening and the antibiotics viomycin and sparsomycin upon the behaviour of bound aatRNA. Decoding at the ribosomal A-site. FEBS Letters, 156, 311-315.
    • (1983) FEBS Letters , vol.156 , pp. 311-315
    • Hornig, H.1    Woolley, P.2    Lührmann, R.3
  • 16
    • 0023139432 scopus 로고
    • 23 S rRNA mutations in Halobacteria conferring resistance to the anti-80 S ribosome targeted antibiotic anisomycin
    • Hummel, H. & Böck, A. (1987). 23 S rRNA mutations in Halobacteria conferring resistance to the anti-80 S ribosome targeted antibiotic anisomycin. Nucl. Acids Res. 15, 2431-2443.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 2431-2443
    • Hummel, H.1    Böck, A.2
  • 17
    • 0002795142 scopus 로고
    • Taxonomy of extremely halophilic bacteria
    • (Rodriguez-Valera, F., ed.), CRC Press, Boca Raton, FA
    • Juez, G. (1988). Taxonomy of extremely halophilic bacteria. In Halophilic Bacteria (Rodriguez-Valera, F., ed.), vol. 2, pp 3-25, CRC Press, Boca Raton, FA.
    • (1988) Halophilic Bacteria , vol.2
    • Juez, G.1
  • 18
    • 0025999638 scopus 로고
    • Chemical, biochemical and genetic endeavours characterizing the interaction of sparsomycin with the ribosome
    • Lázaro, E., van den Broek, L. A. G. M., San Felix, A., Ottenheijm, H. C. J. & Ballesta, J. P. G. (1991a). Chemical, biochemical and genetic endeavours characterizing the interaction of sparsomycin with the ribosome. Biochimie, 73, 1137-1143.
    • (1991) Biochimie , vol.73 , pp. 1137-1143
    • Lázaro, E.1    Van Den Broek, L.A.G.M.2    San Felix, A.3    Ottenheijm, H.C.J.4    Ballesta, J.P.G.5
  • 19
    • 0026008858 scopus 로고
    • Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes
    • Lázaro, E., van den Broek, L. A. G. M., San Felix, A., Ottenheijm, H. C. J. & Ballesta, J. P. G. (1991b). Biochemical and kinetic characteristics of the interaction of the antitumor antibiotic sparsomycin with prokaryotic and eukaryotic ribosomes. Biochemistry, 30, 9642-9648.
    • (1991) Biochemistry , vol.30 , pp. 9642-9648
    • Lázaro, E.1    Van Den Broek, L.A.G.M.2    San Felix, A.3    Ottenheijm, H.C.J.4    Ballesta, J.P.G.5
  • 20
    • 0028269333 scopus 로고
    • A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin a universal inhibitor of peptide bond formation
    • Leviev, I., Rodriguez-Fonseca, C., Phan, H., Garrett, R. A., Heilek, G., Mankin, A. S. & Noller, H. F. (1994). A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin a universal inhibitor of peptide bond formation. EMBO J. 13, 1682-1686.
    • (1994) EMBO J. , vol.13 , pp. 1682-1686
    • Leviev, I.1    Rodriguez-Fonseca, C.2    Phan, H.3    Garrett, R.A.4    Heilek, G.5    Mankin, A.S.6    Noller, H.F.7
  • 21
    • 0025580878 scopus 로고
    • The numerous modified nucleotides in eukaryotic rRNA
    • Maden, B. E. H. (1990). The numerous modified nucleotides in eukaryotic rRNA. Prog. Nucl. Acids Res. Mol. Biol. 39, 241-303.
    • (1990) Prog. Nucl. Acids Res. Mol. Biol. , vol.39 , pp. 241-303
    • Maden, B.E.H.1
  • 22
    • 0025892855 scopus 로고
    • Chloramphenicol resistance mutations in the single 23 S rRNA gene of the archaeon Halobacterium halobium
    • Mankin, A. S. & Garrett, R. A. (1991). Chloramphenicol resistance mutations in the single 23 S rRNA gene of the archaeon Halobacterium halobium. J. Bacteriol. 173, 3559-3563.
    • (1991) J. Bacteriol. , vol.173 , pp. 3559-3563
    • Mankin, A.S.1    Garrett, R.A.2
  • 23
    • 0022572078 scopus 로고
    • Complete nucleotide sequence of the single rRNA operon of Halobacterium halobium: Secondary structure of the archaebacterial 23 S rRNA
    • Mankin, A. S. & Kagramanova, V. K. (1986). Complete nucleotide sequence of the single rRNA operon of Halobacterium halobium: secondary structure of the archaebacterial 23 S rRNA. Mol. Gen. Genet. 202, 152-161.
    • (1986) Mol. Gen. Genet. , vol.202 , pp. 152-161
    • Mankin, A.S.1    Kagramanova, V.K.2
  • 24
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23 S rRNA in the ribosomal A, P and E sites
    • Moazed, D. & Noller, H. F. (1989). Interaction of tRNA with 23 S rRNA in the ribosomal A, P and E sites. Cell, 57, 585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 25
    • 0025811850 scopus 로고
    • Sites of interaction of the -CCA end of peptidyl-tRNA with 23 S rRNA
    • Moazed, D. & Noller, H. F. (1991). Sites of interaction of the -CCA end of peptidyl-tRNA with 23 S rRNA. Proc. Natl Acad. Sci. USA, 88, 3725-3728.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3725-3728
    • Moazed, D.1    Noller, H.F.2
  • 26
    • 0014219788 scopus 로고
    • Ribosome-catalyzed peptidyl transfer: Some inhibitors of protein synthesis
    • Monro, R. & Vázquez, D. (1967). Ribosome-catalyzed peptidyl transfer: some inhibitors of protein synthesis. J. Mol. Biol. 28, 161-165.
    • (1967) J. Mol. Biol. , vol.28 , pp. 161-165
    • Monro, R.1    Vázquez, D.2
  • 27
    • 0014691601 scopus 로고
    • Action of sparsomycin on ribosome catalysed peptidyl transfer
    • Monro, R. E., Celma, M. L., & Vázquez, D. (1969). Action of sparsomycin on ribosome catalysed peptidyl transfer. Nature, 222, 356-358.
    • (1969) Nature , vol.222 , pp. 356-358
    • Monro, R.E.1    Celma, M.L.2    Vázquez, D.3
  • 28
    • 0025733603 scopus 로고
    • rRNA and translation
    • Noller, H. F. (1991). rRNA and translation. Annu. Rev. Biochem. 60, 191-227.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 191-227
    • Noller, H.F.1
  • 30
    • 0021114894 scopus 로고
    • Affinity labeling of the peptidyl transferase center using the 3′-terminal pentanucleotide from amino acyl-tRNA
    • Perez-Gosalbez, M., Leon Rivera, G. & Ballesta, J. P. G. (1983). Affinity labeling of the peptidyl transferase center using the 3′-terminal pentanucleotide from amino acyl-tRNA. Biochem. Biophys. Res. Commun. 113, 941-947.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 941-947
    • Perez-Gosalbez, M.1    Leon Rivera, G.2    Ballesta, J.P.G.3
  • 31
    • 0014584316 scopus 로고
    • Studies on the formation of tRNA-ribosome complexes. XI. Antibiotic effects on phenylalanyl-oligonucleotide binding to ribosomes
    • Pestka, S. (1969). Studies on the formation of tRNA-ribosome complexes. XI. Antibiotic effects on phenylalanyl-oligonucleotide binding to ribosomes. Proc. Natl Acad. Sci. USA, 64, 709-714.
    • (1969) Proc. Natl Acad. Sci. USA , vol.64 , pp. 709-714
    • Pestka, S.1
  • 32
    • 0026591728 scopus 로고
    • Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit E. coli ribosomes during translation
    • Picking, W. D., Picking, W. L., Odom, O. W. & Hardesty, B. (1992). Fluorescence characterization of the environment encountered by nascent polyalanine and polyserine as they exit E. coli ribosomes during translation. Biochemistry, 31, 2368-2375.
    • (1992) Biochemistry , vol.31 , pp. 2368-2375
    • Picking, W.D.1    Picking, W.L.2    Odom, O.W.3    Hardesty, B.4
  • 33
    • 0029011424 scopus 로고
    • Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach
    • Porse, B. & Garrett, R. A. (1995). Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach. J. Mol. Biol. 249, 1-10.
    • (1995) J. Mol. Biol. , vol.249 , pp. 1-10
    • Porse, B.1    Garrett, R.A.2
  • 34
    • 0029403050 scopus 로고
    • Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity
    • Porse, B., Rodriguez-Fonseca, C., Leviev, I. & Garrett, R. A. (1995). Antibiotic inhibition of the movement of tRNA substrates through a peptidyl transferase cavity. Biochem. Cell Biol. 73, 877-885.
    • (1995) Biochem. Cell Biol. , vol.73 , pp. 877-885
    • Porse, B.1    Rodriguez-Fonseca, C.2    Leviev, I.3    Garrett, R.A.4
  • 35
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca, C., Amils, R. & Garrett, R. A. (1995). Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J. Mol. Biol. 247, 224-235.
    • (1995) J. Mol. Biol. , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 38
    • 0024227741 scopus 로고
    • Photo-affinity labelling at the peptidyl transfer centre reveals two different positions for the A and P sites in domain V of 23 S rRNA
    • Steiner, G., Keuchler, E. & Barta, A. (1988). Photo-affinity labelling at the peptidyl transfer centre reveals two different positions for the A and P sites in domain V of 23 S rRNA. EMBO J. 7, 3949-3935.
    • (1988) EMBO J. , vol.7 , pp. 3949-13935
    • Steiner, G.1    Keuchler, E.2    Barta, A.3
  • 39
    • 0030590258 scopus 로고    scopus 로고
    • Site of interaction of sparsomycin, a universal inhibitor of peptidyl transferase, with the ribosome
    • Tan, G. T., DeBlasio, A. & Mankin, A. S. (1996). Site of interaction of sparsomycin, a universal inhibitor of peptidyl transferase, with the ribosome. J. Mol. Biol. 261, 222-230.
    • (1996) J. Mol. Biol. , vol.261 , pp. 222-230
    • Tan, G.T.1    DeBlasio, A.2    Mankin, A.S.3
  • 40
    • 0020366983 scopus 로고
    • Iodination of biological samples without loss of functional activity
    • Tejedor, F. & Ballesta, J. P. G. (1982). Iodination of biological samples without loss of functional activity. Anal. Biochem. 127, 143-149.
    • (1982) Anal. Biochem. , vol.127 , pp. 143-149
    • Tejedor, F.1    Ballesta, J.P.G.2
  • 41
    • 0023131701 scopus 로고
    • Structure-activity relationships of sparsomycin and its analogues. Inhibition of peptide bond formation in cell free systems and of L1210 and bacterial cell growth
    • van den Broek, L. A. G. M., Liskamp, R. M. J., Colstee, H., Lelieveld, P., Remacha, M., Vázquez, D., Ballesta, J. P. G. & Ottenheijm, H. C. J. (1987). Structure-activity relationships of sparsomycin and its analogues. Inhibition of peptide bond formation in cell free systems and of L1210 and bacterial cell growth. J. Med. Chem. 30, 325-333.
    • (1987) J. Med. Chem. , vol.30 , pp. 325-333
    • Van Den Broek, L.A.G.M.1    Liskamp, R.M.J.2    Colstee, H.3    Lelieveld, P.4    Remacha, M.5    Vázquez, D.6    Ballesta, J.P.G.7    Ottenheijm, H.C.J.8
  • 42
    • 19244385826 scopus 로고
    • Inhibitors of protein synthesis
    • Vázquez, D. (1979). Inhibitors of protein synthesis. Mol. Biol. Biochem. Biophys. 30, 1-312.
    • (1979) Mol. Biol. Biochem. Biophys. , vol.30 , pp. 1-312
    • Vázquez, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.