O'Leary N E, Cheema I R, Moore K, Mehard W B, Buse M G
Biochem Biophys Res Commun. 1987 Apr 14;144(1):329-36. doi: 10.1016/s0006-291x(87)80514-4.
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.
从大鼠骨骼肌中纯化得到的组蛋白H1是无细胞体系(兔网织红细胞裂解物)中肽链起始的一种相对有效的抑制剂(在约0.4微摩尔时抑制率达50%)。H1不抑制三元复合物的形成及其与40S核糖体的结合;这些数据与H1结合mRNA相符。这种抑制表现出mRNA选择性:β-珠蛋白mRNA的翻译比α-珠蛋白mRNA更易受影响,肝白蛋白mRNA的翻译比总肝mRNA更易受影响。组蛋白H1在完整细胞的翻译调控中是否起作用尚无定论,它可能是蛋白质-mRNA相互作用的一个有用模型。