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PMID: 3112158 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Missense misreading of asparagine codons as a function of codon identity and context.

The Journal of biological chemistry ·Vol. 262 ·No. 23 ·1987-08-15 ·Pages 11351-5

Precup J, Parker J

Abstract

During asparagine starvation the frequency of lysine for asparagine substitutions increases to levels that enable one to isolate and sequence mistranslated protein. We have used site-directed mutagenesis to construct a series of derivatives of the gene encoding the coat protein of the bacteriophage MS2. The mutant set constructed has either AAU or AAC as codon three in the gene with each possible adjoining 3' base. Lysine incorporation in coat protein encoded by these genes shows that AAU is misread from 4- to 9-fold more frequently than AAC with any 3' context. Although in some cases context effects of approximately 2-fold were noted, there seems to be no simple hypothesis to explain them.

MeSH Terms
Asparagine/genetics Bacteriophages/genetics Base Sequence Capsid/genetics Capsid Proteins Cloning, Molecular Codon DNA, Recombinant Escherichia coli/genetics,physiology Lysine/genetics Mutation Plasmids Protein Biosynthesis RNA, Messenger RNA-Binding Proteins Transcription, Genetic
Chemicals
Capsid Proteins Codon DNA, Recombinant RNA, Messenger RNA-Binding Proteins Asparagine Lysine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Precup J
Parker J
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1987-08-15
Pages
11351-5
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM25855 · United States
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