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Volumn 131, Issue 40, 2009, Pages 14240-14242

Impact of nonnatural amino acid mutagenesis on the in vivo function and binding modes of a transcriptional activator

Author keywords

[No Author keywords available]

Indexed keywords

BINDING INTERFACE; BINDING MODES; BINDING PARTNERS; BIOLOGICAL NETWORKS; CELLULAR FUNCTION; GROWTH CONDITIONS; IN-VIVO; INHIBITOR PROTEINS; KEY BINDING; L-PHENYLALANINE; NON NATURAL AMINO ACIDS; PROTEIN-PROTEIN INTERACTIONS; S.CEREVISIAE; SMALL MOLECULES; SUPPRESSION SYSTEMS; TRANSCRIPTIONAL ACTIVATION DOMAIN; TRANSCRIPTIONAL ACTIVATORS; TRANSCRIPTIONAL ACTIVITY;

EID: 70349923890     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja904378z     Document Type: Article
Times cited : (33)

References (37)
  • 10
    • 55749095055 scopus 로고    scopus 로고
    • A distinct tRNA/synthetase pair for pBpa incorporation in S. cerevisiae and its application to TBP in vitro and in vivo
    • A distinct tRNA/synthetase pair for pBpa incorporation in S. cerevisiae and its application to TBP in vitro and in vivo: Mohibullah, N.; Hahn, S. Genes Dev. 2008, 22, 2994-3006.
    • (2008) Genes Dev. , vol.22 , pp. 2994-3006
    • Mohibullah, N.1    Hahn, S.2
  • 11
    • 0345849436 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory: New York
    • Ptashne, M.; Gann, A. Genes & Signals; Cold Spring Harbor Laboratory: New York, 2001.
    • (2001) Genes & Signals
    • Ptashne, M.1    Gann, A.2
  • 35
    • 70349954644 scopus 로고    scopus 로고
    • note
    • In absence of pBpa, two outcomes are observed: incorporation of a natural amino acid produces full-length protein with an undefined mutation ('readthrough') or, more commonly, the amber codon is interpreted as a 'stop' and a truncated protein is produced. The absolute and relative yields of these two products varies from mutant to mutant.
  • 36
    • 33644886015 scopus 로고    scopus 로고
    • In this instance, the benzophenone moiety may be poorly positioned for cross-linking, particularly as the efficiency of benzophenone cross-linking is well-known to vary with amino acid identity
    • In this instance, the benzophenone moiety may be poorly positioned for cross-linking, particularly as the efficiency of benzophenone cross-linking is well-known to vary with amino acid identity. Wittelsberger, A.; Thomas, B. E.; Mierke, D. F.; Rosenblatt, M. FEBS Lett. 2006, 580, 1872-1876
    • (2006) FEBS Lett. , vol.580 , pp. 1872-1876
    • Wittelsberger, A.1    Thomas, B.E.2    Mierke, D.F.3    Rosenblatt, M.4
  • 37
    • 70349943692 scopus 로고    scopus 로고
    • note
    • An additional contributor to attenuated cross-linking of the Trp840pBpa mutant may be the reduced expression level of this construct (Fig 3a).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.