A Gripping Tale of Ribosomal Frameshifting: Extragenic Suppressors of Frameshift Mutations Spotlight P-Site Realignment

被引:107
作者
Atkins, John F. [1 ,2 ]
Bjork, Glenn R. [3 ]
机构
[1] Univ Utah, Dept Human Genet, Salt Lake City, UT 84112 USA
[2] Natl Univ Ireland Univ Coll Cork, BioSci Inst, Cork, Ireland
[3] Umea Univ, Dept Mol Biol, SE-90187 Umea, Sweden
基金
美国国家卫生研究院; 爱尔兰科学基金会;
关键词
NONNATURAL AMINO-ACIDS; TRANSFER-RIBONUCLEIC-ACID; PEPTIDYL-TRANSFER-RNA; ELONGATION-FACTOR-TU; GLYCINE TRANSFER-RNA; RELEASE FACTOR-II; OPEN READING FRAME; MESSENGER-RNA; ESCHERICHIA-COLI; ANTICODON LOOP;
D O I
10.1128/MMBR.00010-08
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Mutants of translation components which compensate for both -1 and +1 frame-shift mutations showed the first evidence for framing malleability. Those compensatory mutants isolated in bacteria and yeast with altered tRNA or protein factors are reviewed here and are considered to primarily cause altered P-site realignment and not altered translocation. Though the first sequenced tRNA mutant which suppressed a +1 frameshift mutation had an extra base in its anticodon loop and led to a textbook "yardstick" model in which the number of anticodon bases determines codon size, this model has long been discounted, although not by all. Accordingly, the reviewed data suggest that reading frame maintenance and translocation are two distinct features of the ribosome. None of the -1 tRNA suppressors have anticodon loops with fewer than the standard seven nucleotides. Many of the tRNA mutants potentially affect tRNA bending and/or stability and can be used for functional assays, and one has the conserved C74 of the 3' CCA substituted. The effect of tRNA modification deficiencies on framing has been particularly informative. The properties of some mutants suggest the use of alternative tRNA anticodon loop stack conformations by individual tRNAs in one translation cycle. The mutant proteins range from defective release factors with delayed decoding of A-site stop codons facilitating P-site frameshifting to altered EF-Tu/EF1 alpha to mutant ribosomal large- and small-subunit proteins L9 and S9. Their study is revealing how mRNA slippage is restrained except where it is programmed to occur and be utilized.
引用
收藏
页码:178 / +
页数:34
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