Open AccessSynthesis of Lens Protein in vitro Role of Methionyl‐tRNAs in the Synthesis of Calf‐Lens α‐Crystallin
Author(s) -
Strous Ger J. A. M.,
Berns Ton J. M.,
Westernen Hanske,
Bloemendal Hans
Publication year - 1972
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1972.tb02070.x
Subject(s) - methionine , reticulocyte , crystallin , polypeptide chain , transfer rna , residue (chemistry) , protein biosynthesis , acetylation , biochemistry , rna , chemistry , biology , stereochemistry , amino acid , gene
The main polypeptide chain of the lens protein α‐crystallin (αA 2 ) is N‐terminally acetylated and contains two methionine residues. The chain is initiated by the incorporation of a methionine residue exclusively donated by methionyl‐tRNA rMet . This N‐terminal methionine is not removed during polypeptide chain synthesis. The internal methionine residue is donated exclusively by one of the methionyl‐tRNA Met species. When lens messenger RNA coding for the αrA 2 chain is translated in a reticulocyte cell‐free system, the newly synthesized polypeptide chain carries an acetylated methionine in the N‐terminal position.