Histone-H1 inhibits translation by reticulocyte lysates with relative mRNA selectivity.
Histone-H1 purified from rat skeletal muscle is a relatively potent inhibitor of peptide chain initiation in a cell free system, the rabbit reticulocyte lysate (50% inhibition at approximately 0.4 microM). H1 does not inhibit formation of the ternary complex nor its attachment to 40S ribosomes; the data are compatible with H1 binding to mRNA. The inhibition shows mRNA selectivity: translation of beta-globin mRNA is more affected than that of alpha-globin mRNA and hepatic albumin mRNA more than total hepatic mRNA. Whether or not histone-H1 plays a role in translational regulation in intact cells is conjectural, it may serve as a useful model for protein-mRNA interactions.
D000818:Animals; D002474:Cell-Free System; D015852:Eukaryotic Initiation Factor-2; D005914:Globins / Q000096:biosynthesis / Q000235:genetics; D006657:Histones / Q000378:metabolism / Q000494:pharmacology*; D066298:In Vitro Techniques; D051379:Mice; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects; D010448:Peptide Initiation Factors / Q000378:metabolism; D014176:Protein Biosynthesis / Q000187:drug effects*; D011506:Proteins / Q000378:metabolism; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism*; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism
D015852:Eukaryotic Initiation Factor-2; D006657:Histones; D010448:Peptide Initiation Factors; D011506:Proteins; D012333:RNA, Messenger; D005914:Globins