메뉴 건너뛰기




Volumn 10, Issue 3, 2004, Pages 482-492

Interaction of the Bacillus subtilis RNase P with the 30S ribosomal subunit

Author keywords

30S subunit; Ribosome; Ribozyme; RNase P

Indexed keywords

AMMONIUM CHLORIDE; CELL EXTRACT; DIMER; HOLOENZYME; HYDROXYL RADICAL; MAGNESIUM CHLORIDE; RIBONUCLEASE P; RIBONUCLEOPROTEIN; RIBOZYME; TRANSFER RNA;

EID: 1242273880     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.5163104     Document Type: Article
Times cited : (26)

References (27)
  • 1
    • 0028568179 scopus 로고
    • Ribonuclease E provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA
    • Alifano, P., Rivellini, F., Piscitelli, C., Arraiano, C.M., Bruni, C.B., and Carlomagno, M.S. 1994. Ribonuclease E provides substrates for ribonuclease P-dependent processing of a polycistronic mRNA. Genes & Dev. 8: 3021-3031.
    • (1994) Genes & Dev. , vol.8 , pp. 3021-3031
    • Alifano, P.1    Rivellini, F.2    Piscitelli, C.3    Arraiano, C.M.4    Bruni, C.B.5    Carlomagno, M.S.6
  • 2
    • 0003120548 scopus 로고    scopus 로고
    • Ribonuclease P
    • (eds. R.F. Gesteland et al.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Altman, S. and Kirsebom, L. 1999. Ribonuclease P. In The RNA world, 2nd ed. (eds. R.F. Gesteland et al.), pp. 351-380. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1999) The RNA World, 2nd Ed. , pp. 351-380
    • Altman, S.1    Kirsebom, L.2
  • 3
    • 0037195276 scopus 로고    scopus 로고
    • Dimeric and monomeric Bacillus subtilis RNase P holoenzyme in the absence and presence of pre-tRNA substrates
    • Barrera, A., Fang, X., Jacob, J., Casey, E., Thiyagarajan, P., Pan, T. 2002. Dimeric and monomeric Bacillus subtilis RNase P holoenzyme in the absence and presence of pre-tRNA substrates. Biochemistry 41: 12986-12994.
    • (2002) Biochemistry , vol.41 , pp. 12986-12994
    • Barrera, A.1    Fang, X.2    Jacob, J.3    Casey, E.4    Thiyagarajan, P.5    Pan, T.6
  • 4
    • 0344298926 scopus 로고    scopus 로고
    • The Ribonuclease P Database
    • Brown, J.W. 1999. The Ribonuclease P Database. Nucleic Acids Res. 27: 314.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 314
    • Brown, J.W.1
  • 5
    • 0032473358 scopus 로고    scopus 로고
    • Comparative photocross-linking analysis of the tertiary structures of Escherichia coli and Bacillus subtilis RNase P RNAs
    • Chen, J.L., Nolan, J.M., Harris, M.E., and Pace, N.R. 1998. Comparative photocross-linking analysis of the tertiary structures of Escherichia coli and Bacillus subtilis RNase P RNAs. EMBO J. 17: 1515-1525.
    • (1998) EMBO J. , vol.17 , pp. 1515-1525
    • Chen, J.L.1    Nolan, J.M.2    Harris, M.E.3    Pace, N.R.4
  • 9
    • 0031711821 scopus 로고    scopus 로고
    • Ribonuclease P: Unity and diversity in a tRNA processing ribozyme
    • Frank, D.N. and Pace, N.R. 1998. Ribonuclease P: Unity and diversity in a tRNA processing ribozyme. Annu. Rev. Biochem. 67: 153-180.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 153-180
    • Frank, D.N.1    Pace, N.R.2
  • 10
    • 0034538974 scopus 로고    scopus 로고
    • Phylogenetic-comparative analysis of the eukaryal ribonuclease P RNA
    • Frank, D.N., Adamidi, C., Ehringer, M.A., Pitulle, C., and Pace, N.R. 2000. Phylogenetic-comparative analysis of the eukaryal ribonuclease P RNA. RNA 6: 1895-1904.
    • (2000) RNA , vol.6 , pp. 1895-1904
    • Frank, D.N.1    Adamidi, C.2    Ehringer, M.A.3    Pitulle, C.4    Pace, N.R.5
  • 11
    • 0016697073 scopus 로고
    • Ribosome-dependent conversion of polyA-containing heterogenous nuclear RNA into smaller RNA molecules
    • Grozdanovic, J. and Hradec, J. 1975. Ribosome-dependent conversion of polyA-containing heterogenous nuclear RNA into smaller RNA molecules. Nucleic Acids Res. 2: 821-830.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 821-830
    • Grozdanovic, J.1    Hradec, J.2
  • 12
    • 0021013526 scopus 로고
    • The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme
    • Guerrier-Takada, C., Gardiner, K., Marsh, T., Pace, N., and Altman, S. 1983. The RNA moiety of ribonuclease P is the catalytic subunit of the enzyme. Cell 35: 849-857.
    • (1983) Cell , vol.35 , pp. 849-857
    • Guerrier-Takada, C.1    Gardiner, K.2    Marsh, T.3    Pace, N.4    Altman, S.5
  • 13
    • 0034944725 scopus 로고    scopus 로고
    • Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis
    • Hansen, A., Pfeiffer, T., Zuleeg, T., Limmer, S., Ciesiolka, J., Feltens, R., and Hartmann, R.K. 2001. Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis. Mol. Microbiol. 41: 131-143.
    • (2001) Mol. Microbiol. , vol.41 , pp. 131-143
    • Hansen, A.1    Pfeiffer, T.2    Zuleeg, T.3    Limmer, S.4    Ciesiolka, J.5    Feltens, R.6    Hartmann, R.K.7
  • 14
    • 0029074106 scopus 로고
    • Precursor of C4 antisense RNA of bacteriophages P1 and P7 is a substrate for RNase P of Escherichia coli
    • Hartmann, R.K., Heinrich, J., Schlegl, J., and Schuster, H. 1995. Precursor of C4 antisense RNA of bacteriophages P1 and P7 is a substrate for RNase P of Escherichia coli. Proc. Natl. Acad. Sci. 92: 5822-5826.
    • (1995) Proc. Natl. Acad. Sci. , vol.92 , pp. 5822-5826
    • Hartmann, R.K.1    Heinrich, J.2    Schlegl, J.3    Schuster, H.4
  • 15
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
    • Keiler, K.C., Waller, P.R., and Sauer, R.T. 1996. Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA. Science 271: 990-993.
    • (1996) Science , vol.271 , pp. 990-993
    • Keiler, K.C.1    Waller, P.R.2    Sauer, R.T.3
  • 16
    • 0037199416 scopus 로고    scopus 로고
    • The affinity of magnesium binding sites in the Bacillus subtilis RNase P x pre-tRNA complex is enhanced by the protein subunit
    • Kurz, J.C. and Fierke, C.A. 2002. The affinity of magnesium binding sites in the Bacillus subtilis RNase P x pre-tRNA complex is enhanced by the protein subunit. Biochemistry 41: 9545-9558.
    • (2002) Biochemistry , vol.41 , pp. 9545-9558
    • Kurz, J.C.1    Fierke, C.A.2
  • 18
    • 0033733794 scopus 로고    scopus 로고
    • The 3′ substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo
    • Loria, A. and Pan, T. 2000. The 3′ substrate determinants for the catalytic efficiency of the Bacillus subtilis RNase P holoenzyme suggest autolytic processing of the RNase P RNA in vivo. RNA 6: 1413-1422.
    • (2000) RNA , vol.6 , pp. 1413-1422
    • Loria, A.1    Pan, T.2
  • 19
    • 0032480795 scopus 로고    scopus 로고
    • Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme
    • Loria, A., Niranjanakumari, S., Fierke, C.A., and Pan, T. 1998. Recognition of a pre-tRNA substrate by the Bacillus subtilis RNase P holoenzyme. Biochemistry 37: 15466-15473.
    • (1998) Biochemistry , vol.37 , pp. 15466-15473
    • Loria, A.1    Niranjanakumari, S.2    Fierke, C.A.3    Pan, T.4
  • 20
    • 0032417685 scopus 로고    scopus 로고
    • Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA
    • Niranjanakumari, S., Stams, T., Crary, S.M., Christianson, D.W., and Fierke, C.A. 1998. Protein component of the ribozyme ribonuclease P alters substrate recognition by directly contacting precursor tRNA. Proc. Natl. Acad. Sci. 95: 15212-15217.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 15212-15217
    • Niranjanakumari, S.1    Stams, T.2    Crary, S.M.3    Christianson, D.W.4    Fierke, C.A.5
  • 21
    • 0025826411 scopus 로고
    • Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli
    • Peck-Miller, K.A. and Altman, S. 1991. Kinetics of the processing of the precursor to 4.5 S RNA, a naturally occurring substrate for RNase P from Escherichia coli. J. Mol. Biol. 221: 1-5.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1-5
    • Peck-Miller, K.A.1    Altman, S.2
  • 22
    • 0022977851 scopus 로고
    • The RNA component of the Bacillus subtilis RNase P. Sequence, activity, and partial secondary structure
    • Reich, C., Gardiner, K.J., Olsen, G.J., Pace, B., Marsh, T.L., and Pace, N.R. 1986. The RNA component of the Bacillus subtilis RNase P. Sequence, activity, and partial secondary structure. J. Biol. Chem. 261: 7888-7893.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7888-7893
    • Reich, C.1    Gardiner, K.J.2    Olsen, G.J.3    Pace, B.4    Marsh, T.L.5    Pace, N.R.6
  • 23
    • 0023865082 scopus 로고
    • Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme
    • Reich, C., Olsen, G.J., Pace, B., and Pace, N.R. 1988. Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme. Science 239: 178-181.
    • (1988) Science , vol.239 , pp. 178-181
    • Reich, C.1    Olsen, G.J.2    Pace, B.3    Pace, N.R.4
  • 24
    • 0015523504 scopus 로고
    • Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid precursor
    • Robertson, H.D., Altman, S., and Smith, J.D. 1972. Purification and properties of a specific Escherichia coli ribonuclease which cleaves a tyrosine transfer ribonucleic acid precursor. J. Biol. Chem. 247: 5243-5251.
    • (1972) J. Biol. Chem. , vol.247 , pp. 5243-5251
    • Robertson, H.D.1    Altman, S.2    Smith, J.D.3
  • 25
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles
    • (ed. G. Spedding). Oxford University Press, Oxford, UK
    • Spedding, G. 1990. Isolation and analysis of ribosomes from prokaryotes, eukaryotes, and organelles. In Ribosomes and Protein Synthesis, a Practical Approach (ed. G. Spedding), pp. 1-29. Oxford University Press, Oxford, UK.
    • (1990) Ribosomes and Protein Synthesis, a Practical Approach , pp. 1-29
    • Spedding, G.1
  • 26
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern, S., Moazed, D., and Noller, H.F. 1988. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol. 164: 481-489.
    • (1988) Methods Enzymol. , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 27
    • 0037462929 scopus 로고    scopus 로고
    • Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme
    • Tsai, H.Y., Masquida, B., Biswas, R., Westhof, E., and Gopalan, V. 2003. Molecular modeling of the three-dimensional structure of the bacterial RNase P holoenzyme. J. Mol. Biol. 325: 661-675.
    • (2003) J. Mol. Biol. , vol.325 , pp. 661-675
    • Tsai, H.Y.1    Masquida, B.2    Biswas, R.3    Westhof, E.4    Gopalan, V.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.