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Volumn 41, Issue 1, 2001, Pages 131-143

Exploring the minimal substrate requirements for trans-cleavage by RNase P holoenzymes from Escherichia coli and Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HOLOENZYME; HYBRID PROTEIN; OLIGONUCLEOTIDE; PROTEIN SUBUNIT; RIBONUCLEASE P; TRANSFER RNA;

EID: 0034944725     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.2001.02467.x     Document Type: Article
Times cited : (43)

References (43)
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    • Loria, A.1    Pan, T.2
  • 24
    • 0032516438 scopus 로고    scopus 로고
    • Recognition of the 5′ leader and the acceptor stem of a pre-tRNA substrate by the ribozyme from Bacillus subtilis RNase P
    • (1998) Biochemistry , vol.37 , pp. 10126-10133
    • Loria, A.1    Pan, T.2
  • 25
    • 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
    • (2000) RNA , vol.6 , pp. 1413-1422
    • Loria, A.1    Pan, T.2
  • 26
    • 0028364761 scopus 로고
    • Differential evolution of substrates for an RNA enzyme in the presence and absence of its protein cofactor
    • (1994) Cell , vol.77 , pp. 1093-1100
    • Liu, F.1    Altman, S.2
  • 30
  • 34
    • 0029025035 scopus 로고
    • Novel RNA substrates for the ribozyme from Bacillus subtilis ribonuclease P identified by in vitro selection
    • (1995) Biochemistry , vol.34 , pp. 8458-8464
    • Pan, T.1
  • 35
    • 0029874464 scopus 로고    scopus 로고
    • Multiple substrate binding sites in the ribozyme from Bacillus subtilis RNase P
    • (1996) EMBO J , vol.15 , pp. 2249-2255
    • Pan, T.1    Jakacka, M.2
  • 37
    • 0025826411 scopus 로고
    • Kinetics of the processing of the precursor to 4.5S RNA, a naturally occurring substrate for RNase P from Escherichia coli
    • (1991) J Mol Biol , vol.221 , pp. 1-5
    • Peck-Miller, K.A.1    Altman, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.