Open AccessSynthesis of Lens Protein in vitro
Author(s) -
Berns Ton J.M.,
Schbeurs Victor V.A.M.,
Kraaikamp Marjolijn W.G.,
Bloemendal Hans
Publication year - 1973
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1973.tb02715.x
Subject(s) - polysome , acetylation , messenger rna , protein biosynthesis , methionine , translation (biology) , biochemistry , in vitro , chemistry , amino acid , lens (geology) , residue (chemistry) , fidelity , rna , biology , ribosome , gene , computer science , paleontology , telecommunications
Messenger ribonucleic acid was isolated from calf lens polyribosomes and fractionated. Previous identifications of the newly synthesized products have been extended in that the fidelity of the translation of the 14‐S mRNA was assayed by fingerprinting analysis. The results suggest that lens messenger is translated with a high degree of fidelity in the cross systems even to the extent that the newly synthesized αA 2 chains contain an acetylated methionine residue in the N‐terminal position like the native chains. There seems to be no requirement for cell‐specific protein factors in order to obtain accurate translation. Evidence is accumulating that the acetylation is not involved in the initiation mechanism.