Thomas J O, Glowacka S K, Szer W
J Mol Biol. 1983 Dec 25;171(4):439-55. doi: 10.1016/0022-2836(83)90039-6.
We have investigated the structure of complexes formed between a series of poly(A)n (n = 30 to 480) and HD40 (helix-destabilizing protein, molecular weight of 40,000), the major protein component of 30 S heterogeneous nuclear ribonucleoprotein particles (hnRNP) from the brine shrimp Artemia salina. Protein HD40 is similar to corresponding hnRNP proteins from higher eukaryotes and the complexes it forms with single-stranded nucleic acids are strikingly similar to the native "beads-on-a-string" structure of hnRNP. Using analytical ultracentrifugation and electron microscopy we find: (1) complexes formed between HD40 and long ribohomopolymers also have a beads-on-a-string structure, showing that the ability to form this structure is an inherent property of HD40, and is not dependent on any structural features of natural RNA; (2) complexes between HD40 and poly(A)160 form disks that are about 3 nm high by 18 nm in diameter and contain 20 HD40 molecules; (3) complexes of HD40 with poly(A)n with fewer than 160 nucleotides form sectors of a disk: 40 nucleotides give rise to a quarter of a disk, 80 nucleotides, half a disk, etc. The molecular weights increase with the size of poly(A)n at the rate of 5300 per nucleotide, a stoichiometry of eight nucleotides per HD40; (4) as the size of the poly(A)n increases beyond 160 nucleotides, the additional nucleoprotein elements may either initiate the formation of a second disk adjacent to the first or stack on top of the first disk to form a 6 nm high helix with a diameter of 18 nm. Based on these results, we propose that the existence of lateral protein-protein interactions that produce the basic 3 nm X 18 nm disk, combined with the marginal stability of the helix result in (a) interruptions of the helix that give rise to the beads-on-a-string appearance of the complexes, and (b) inherent heterogeneity of individual "beads" which may contain one or more turns of the helix. From measurements of HD40 complexes with coliphage MS2 RNA, phi X174 viral DNA as well as with the homopolymers, a bead is estimated to contain an average of approximately 300 nucleotides; approximately 1 X 8 turns of the helix.
我们研究了一系列聚(A)n(n = 30至480)与HD40(解螺旋蛋白,分子量为40,000)形成的复合物的结构,HD40是卤虫无节幼体30S异质核核糖核蛋白颗粒(hnRNP)的主要蛋白质成分。蛋白质HD40与来自高等真核生物的相应hnRNP蛋白质相似,它与单链核酸形成的复合物与hnRNP的天然“串珠”结构惊人地相似。使用分析超速离心和电子显微镜,我们发现:(1)HD40与长核糖同聚物形成的复合物也具有串珠结构,表明形成这种结构的能力是HD40的固有特性,并且不依赖于天然RNA的任何结构特征;(2)HD40与聚(A)160形成的复合物形成直径约18nm、高约3nm的圆盘,包含20个HD40分子;(3)HD40与少于160个核苷酸的聚(A)n形成的复合物形成圆盘的扇形:40个核苷酸产生圆盘的四分之一,80个核苷酸产生圆盘的一半等。分子量随着聚(A)n的大小以每核苷酸5300的速率增加,化学计量比为每个HD40八个核苷酸;(4)随着聚(A)n的大小增加超过160个核苷酸,额外的核蛋白元件可能会引发与第一个圆盘相邻的第二个圆盘的形成,或者堆叠在第一个圆盘之上形成直径为18nm、高6nm的螺旋体。基于这些结果,我们提出产生基本的3nm×18nm圆盘的横向蛋白质 - 蛋白质相互作用的存在,与螺旋体的边缘稳定性相结合,导致(a)螺旋体的中断,从而产生复合物的串珠外观,以及(b)单个“珠子”的固有异质性,其可能包含螺旋体的一圈或多圈。通过测量HD40与噬菌体MS2 RNA、φX174病毒DNA以及同聚物的复合物,估计一个珠子平均包含约300个核苷酸;大约1×8圈螺旋体。