Normal tRNAs promote ribosomal frameshifting

Atkins, J. F., Gesteland, R. F., Reid, B. R., Anderson, C. W. (December 1979) Normal tRNAs promote ribosomal frameshifting. Cell, 18 (4). pp. 1119-31. ISSN 0092-8674 (Print)0092-8674 (Linking)

URL: http://www.ncbi.nlm.nih.gov/pubmed/391405
DOI: 10.1016/0092-8674(79)90225-3

Abstract

The addition of Ser AGC AGU tRNA to an E. coli cell-free protein synthesizing system which contains the endogenous tRNA levels results in up to 100% of the ribosomes translating the MS2 coat gene shifting into the -1 reading frame. An analogous phenomenon is seen at a much lower level without the tRNA addition, where a shift into the +1 frame can also be detected. Thus translation with the endogenous tRNA levels yields proteins which have the amino terminus of the coat protein but which are substantially larger than the coat protein and comprise about 5% of the coat translation. Since the lysis gene overlaps the 3' end of the coat gene in the +1 frame, we conclude that the reading frame shift into the +1 frame yields a hybrid protein. Also, we present evidence that ribosomes translating the synthetase gene shift into the -1 frame near the distal end of the gene. This frameshifting is promoted by thrACU ACC tRNA. Specific competitor tRNAs for both Thr and Ser tRNA-promoted frameshifting have been characterized. The generality of this new mechanism for producing additional proteins is unclear, but it investigation should increase understanding of the coding mechanism and its origin.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Codon Coliphages Escherichia coli *Protein Biosynthesis RNA, Bacterial/*physiology RNA, Transfer/*physiology Ribosomes/*physiology Templates, Genetic Viral Proteins/analysis/*biosynthesis
Subjects: organism description > bacteria > escherichia coli
organs, tissues, organelles, cell types and functions > organelles, types and functions > ribosome
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > tRNA
CSHL Authors:
Communities: CSHL labs
Depositing User: Matt Covey
Date: December 1979
Date Deposited: 10 Aug 2016 19:44
Last Modified: 10 Aug 2016 19:44
Related URLs:
URI: http://repository.cshl.edu/id/eprint/32653

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