Regulation of gene expression by stop codon recoding: selenocysteine

被引:59
作者
Copeland, PR [1 ]
机构
[1] Univ Med & Dent New Jersey, Robert Wood Johnson Med Sch, Dept Mol Genet Microbiol & Immunol, Piscataway, NJ 08854 USA
关键词
translation; initiation; elongation; termination; selenocysteine insertion sequence (SECIS); SECIS binding protein;
D O I
10.1016/S0378-1119(03)00588-2
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The regulation of gene expression at the translational level not only allows for rapid changes in specific protein levels but also provides an opportunity to alter codon specificity. For the incorporation of selenocysteine (Sec) into protein, the UGA codon is transformed from one that signals translation termination to one specific for Sec. This review provides a look at Sec incorporation from the perspective of the individual steps involved in protein synthesis: initiation, elongation and termination. The roles of the factors known to be required for Sec incorporation are considered in the context of each step in translation including structural modeling of the differences between the standard elongation factor eEF1A and the Sec-specific counterpart, eEFSec. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:17 / 25
页数:9
相关论文
共 54 条
  • [1] Translation elongation factor 1 functions in the yeast Saccharomyces cerevisiae
    Anand, M
    Valente, L
    Carr-Schmid, A
    Munshi, R
    Olarewaju, O
    Ortiz, PA
    Kinzy, TG
    [J]. COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 2001, 66 : 439 - 448
  • [2] Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Bα
    Andersen, GR
    Pedersen, L
    Valente, L
    Chatterjee, I
    Kinzy, TG
    Kjeldgaard, M
    Nyborg, J
    [J]. MOLECULAR CELL, 2000, 6 (05) : 1261 - 1266
  • [3] Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Bα complex
    Andersen, GR
    Valente, L
    Pedersen, L
    Kinzy, TG
    Nyborg, J
    [J]. NATURE STRUCTURAL BIOLOGY, 2001, 8 (06) : 531 - 534
  • [4] Selenocysteine incorporation directed from the 3'UTR: Characterization of eukaryotic EFsec and mechanistic implications
    Berry, MJ
    Tujebajeva, RM
    Copeland, PR
    Xu, XM
    Carlson, BA
    Martin, GW
    Low, SC
    Mansell, JB
    Grundner-Culemann, E
    Harney, JW
    Driscoll, DM
    Hatfield, DL
    [J]. BIOFACTORS, 2001, 14 (1-4) : 17 - 24
  • [5] Early embryonic lethality caused by targeted disruption of the mouse selenocysteine tRNA gene (Trsp)
    Bosl, MR
    Takaku, K
    Oshima, M
    Nishimura, S
    Taketo, MM
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (11) : 5531 - 5534
  • [6] The polypeptide chain release factor eRF1 specifically contacts the s4UGA stop codon located in the A site of eukaryotic ribosomes
    Chavatte, L
    Frolova, L
    Kisselev, L
    Favre, A
    [J]. EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (10): : 2896 - 2904
  • [7] A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs
    Copeland, PR
    Fletcher, JE
    Carlson, BA
    Hatfield, DL
    Driscoll, DM
    [J]. EMBO JOURNAL, 2000, 19 (02) : 306 - 314
  • [8] Purification, redox sensitivity, and RNA binding properties of SECIS-binding protein 2, a protein involved in selenoprotein biosynthesis
    Copeland, PR
    Driscoll, DM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (36) : 25447 - 25454
  • [9] RNA binding proteins and selenocysteine
    Copeland, PR
    Driscoll, DM
    [J]. BIOFACTORS, 2001, 14 (1-4) : 11 - 16
  • [10] Insight into mammalian selenocysteine insertion: Domain structure and ribosome binding properties of Sec insertion sequence binding protein 2
    Copeland, PR
    Stepanik, VA
    Driscoll, DM
    [J]. MOLECULAR AND CELLULAR BIOLOGY, 2001, 21 (05) : 1491 - 1498