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Volumn 31, Issue 9, 2003, Pages 2272-2278

A candidate prostate cancer susceptibility gene encodes tRNA 3′ processing endoribonuclease

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ARGININE; COMPLEMENTARY DNA; ENZYME VARIANT; ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN; RIBONUCLEASE; RNA PRECURSOR; TRANSFER RNA; 3' PRE TRNASE; 3'-PRE-TRNASE; ARGININE TRANSFER RNA; ELAC2 PROTEIN, HUMAN; TUMOR PROTEIN;

EID: 0038750928     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg337     Document Type: Article
Times cited : (158)

References (30)
  • 7
    • 0031728459 scopus 로고    scopus 로고
    • A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases
    • Melino,S., Capo,C., Dragani,B., Aceto,A. and Petruzzelli,R. (1998) A zinc-binding motif conserved in glyoxalase II, beta-lactamase and arylsulfatases. Trends Biol. Sci., 23, 381-382.
    • (1998) Trends Biol. Sci. , vol.23 , pp. 381-382
    • Melino, S.1    Capo, C.2    Dragani, B.3    Aceto, A.4    Petruzzelli, R.5
  • 8
    • 0028125162 scopus 로고
    • A single amino acid change in SNM1-encoded protein leads to thermoconditional deficiency for DNA cross-link repair in Saccharomyces cerevisiae
    • Niegemann,E. and Brendel,M. (1994) A single amino acid change in SNM1-encoded protein leads to thermoconditional deficiency for DNA cross-link repair in Saccharomyces cerevisiae. Mutat. Res., 315, 275-279.
    • (1994) Mutat. Res. , vol.315 , pp. 275-279
    • Niegemann, E.1    Brendel, M.2
  • 9
    • 0034832844 scopus 로고    scopus 로고
    • This is the end: Processing, editing and repair at the tRNA 3′-terminus
    • Schurer,H., Schiffer,S., Marchfelder,A. and Morl,M. (2001) This is the end: processing, editing and repair at the tRNA 3′-terminus. Biol. Chem., 382, 1147-1156.
    • (2001) Biol. Chem. , vol.382 , pp. 1147-1156
    • Schurer, H.1    Schiffer, S.2    Marchfelder, A.3    Morl, M.4
  • 10
    • 0029113672 scopus 로고
    • Conversion of mammalian tRNA 3′ processing endoribonuclease to four-base-recognizing RNA cutters
    • Nashimoto,M. (1995) Conversion of mammalian tRNA 3′ processing endoribonuclease to four-base-recognizing RNA cutters. Nucleic Acids Res., 23, 3642-3647.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3642-3647
    • Nashimoto, M.1
  • 11
    • 0030754921 scopus 로고    scopus 로고
    • Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease
    • Nashimoto,M. (1997) Distribution of both lengths and 5′ terminal nucleotides of mammalian pre-tRNA 3′ trailers reflects properties of 3′ processing endoribonuclease. Nucleic Acids Res., 25, 1148-1155.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1148-1155
    • Nashimoto, M.1
  • 12
    • 0033537798 scopus 로고    scopus 로고
    • Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M., Tamura,M. and Kaspar,R.L. (1999) Selection of cleavage site by mammalian tRNA 3′ processing endoribonuclease. J. Mol. Biol., 287, 727-740.
    • (1999) J. Mol. Biol. , vol.287 , pp. 727-740
    • Nashimoto, M.1    Tamura, M.2    Kaspar, R.L.3
  • 13
    • 0033554375 scopus 로고    scopus 로고
    • Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M., Tamura,M. and Kaspar,R.L. (1999) Minimum requirements for substrates of mammalian tRNA 3′ processing endoribonuclease. Biochemistry, 38, 12089-12096.
    • (1999) Biochemistry , vol.38 , pp. 12089-12096
    • Nashimoto, M.1    Tamura, M.2    Kaspar, R.L.3
  • 14
    • 0033168104 scopus 로고    scopus 로고
    • Long 5′ leaders inhibit removal of a 3′ trailer from a precursor tRNA by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M., Wesemann,D.R., Geary,S., Tamura,M. and Kaspar,R.L. (1999) Long 5′ leaders inhibit removal of a 3′ trailer from a precursor tRNA by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 27, 2770-2776.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2770-2776
    • Nashimoto, M.1    Wesemann, D.R.2    Geary, S.3    Tamura, M.4    Kaspar, R.L.5
  • 15
    • 0025816716 scopus 로고
    • A novel spermidine-dependent endoribonuclease activity caused by RNA-protein complex in mouse FM3A cell extracts
    • Nashimoto,M., Kominami,R., Nishi,S. and Mishima,Y. (1991) A novel spermidine-dependent endoribonuclease activity caused by RNA-protein complex in mouse FM3A cell extracts. Biochem. Biophys. Res. Commun., 176, 1163-1169.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1163-1169
    • Nashimoto, M.1    Kominami, R.2    Nishi, S.3    Mishima, Y.4
  • 16
    • 0026752809 scopus 로고
    • Characterization of the spermidine-dependent, sequence-specific endoribonuclease that requires transfer RNA for its activity
    • Nashimoto,M. (1992) Characterization of the spermidine-dependent, sequence-specific endoribonuclease that requires transfer RNA for its activity. Nucleic Acids Res., 20, 3737-3742.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3737-3742
    • Nashimoto, M.1
  • 17
    • 0027340664 scopus 로고
    • Arg is essential for in vitro specific cleavage of partially synthesized mouse 18S rRNA
    • Arg is essential for in vitro specific cleavage of partially synthesized mouse 18S rRNA. Nucleic Acids Res., 21, 4696-4702.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4696-4702
    • Nashimoto, M.1
  • 18
    • 0029854010 scopus 로고    scopus 로고
    • Specific cleavage of target RNAs from HIV-1 with 5′ half tRNA by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M. (1996) Specific cleavage of target RNAs from HIV-1 with 5′ half tRNA by mammalian tRNA 3′ processing endoribonuclease. RNA, 2, 523-534.
    • (1996) RNA , vol.2 , pp. 523-534
    • Nashimoto, M.1
  • 19
    • 0032103908 scopus 로고    scopus 로고
    • RNA heptamers that direct RNA cleavage by mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M., Geary,S., Tamura,M. and Kaspar,R. (1998) RNA heptamers that direct RNA cleavage by mammalian tRNA 3′ processing endoribonuclease. Nucleic Acids Res., 26, 2565-2571.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2565-2571
    • Nashimoto, M.1    Geary, S.2    Tamura, M.3    Kaspar, R.4
  • 20
    • 0034725035 scopus 로고    scopus 로고
    • Anomalous RNA substrates for mammalian tRNA 3′ processing endoribonuclease
    • Nashimoto,M. (2000) Anomalous RNA substrates for mammalian tRNA 3′ processing endoribonuclease. FEBS Lett., 472, 179-186.
    • (2000) FEBS Lett. , vol.472 , pp. 179-186
    • Nashimoto, M.1
  • 21
    • 0036788304 scopus 로고    scopus 로고
    • Gene silencing in mammals by small interfering RNAs
    • McManus,M.T. and Sharp,P.A. (2002) Gene silencing in mammals by small interfering RNAs. Nature Rev. Genet., 3, 737-747.
    • (2002) Nature Rev. Genet. , vol.3 , pp. 737-747
    • McManus, M.T.1    Sharp, P.A.2
  • 22
    • 0035812598 scopus 로고    scopus 로고
    • The inhibitory effect of the autoantigen La on in vitro 3′ processing of mammalian precursor tRNAs
    • Nashimoto,M., Nashimoto,C., Tamura,M., Kaspar,R.L. and Ochi,K. (2001) The inhibitory effect of the autoantigen La on in vitro 3′ processing of mammalian precursor tRNAs. J. Mol. Biol., 312, 975-984.
    • (2001) J. Mol. Biol. , vol.312 , pp. 975-984
    • Nashimoto, M.1    Nashimoto, C.2    Tamura, M.3    Kaspar, R.L.4    Ochi, K.5
  • 23
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho,S.N., Hunt,H.D., Horton,R.M., Pullen,J.K. and Pease,L.R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 24
    • 0018459544 scopus 로고
    • Direct chemical method for sequencing RNA
    • Peattie,D.A. (1979) Direct chemical method for sequencing RNA. Proc. Natl Acad. Sci. USA, 76, 1760-1764.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1760-1764
    • Peattie, D.A.1
  • 25
    • 0030436198 scopus 로고    scopus 로고
    • Pre-tRNA 3′-processing in Saccharomyces cerevisiae. Purification and characterization of exo- and endoribonucleases
    • Papadimitriou,A. and Gross,H.J. (1996) Pre-tRNA 3′-processing in Saccharomyces cerevisiae. Purification and characterization of exo- and endoribonucleases. Eur. J. Biochem., 242, 747-759.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 747-759
    • Papadimitriou, A.1    Gross, H.J.2
  • 26
    • 0030904723 scopus 로고    scopus 로고
    • The yeast La protein is required for the 3′ endonucleolytic cleavage that matures tRNA precursors
    • Yoo,C.J. and Wolin,S.L. (1997) The yeast La protein is required for the 3′ endonucleolytic cleavage that matures tRNA precursors. Cell, 89, 393-402.
    • (1997) Cell , vol.89 , pp. 393-402
    • Yoo, C.J.1    Wolin, S.L.2
  • 27
    • 0037013852 scopus 로고    scopus 로고
    • Assigning a function to a conserved group of proteins: The tRNA 3′-processing enzymes
    • Schiffer,S., Rosch,S. and Marchfelder,A. (2002) Assigning a function to a conserved group of proteins: the tRNA 3′-processing enzymes. EMBO J., 21, 2769-2777.
    • (2002) EMBO J. , vol.21 , pp. 2769-2777
    • Schiffer, S.1    Rosch, S.2    Marchfelder, A.3
  • 29
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker,J.E., Saraste,M., Runswick,M.J. and Gay,N.J. (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J., 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 30
    • 0037431434 scopus 로고    scopus 로고
    • The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the γ-tubulin complex
    • Korver,W., Guevara,C., Chen,Y., Neuteboom,S., Bookstein,R., Tavtigian,S. and Lees,E. (2003) The product of the candidate prostate cancer susceptibility gene ELAC2 interacts with the γ-tubulin complex. Int. J. Cancer, 104, 283-298.
    • (2003) Int. J. Cancer , vol.104 , pp. 283-298
    • Korver, W.1    Guevara, C.2    Chen, Y.3    Neuteboom, S.4    Bookstein, R.5    Tavtigian, S.6    Lees, E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.