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腺病毒蛋白VII(一种混合碱性染色体蛋白)的基因和蛋白质序列

Gene and protein sequences of adenovirus protein VII, a hybrid basic chromosomal protein.

作者信息

Sung M T, Cao T M, Coleman R T, Budelier K A

出版信息

Proc Natl Acad Sci U S A. 1983 May;80(10):2902-6. doi: 10.1073/pnas.80.10.2902.

Abstract

The sequences of both the gene and the corresponding protein of adenovirus major core protein VII have been determined. The precise location of this gene is between 43.37 and 44.90 map coordinates on the viral genome. Protein VII is 173 residues long and has a molecular weight of 19,258. Detailed analysis of its sequence has revealed four basic domains separated by several predicted alpha helices. It is proposed that intrachain folding of protein VII is driven by hydrophobic interactions of the alpha helices, leaving the basic domains of the protein to interact with DNA phosphates. Protein monomers may further associate with each other in the formation of hexameric nucleosome-like particles. The displacement and replacement of protein VII during the viral infectious cycle in the host cell appears to mimic the biology of nucleoprotamine during the processes of spermatogenesis and fertilization. The presence of a protamine-like domain affirms a hybrid histone/protamine molecular structure for protein VII, although it may resemble the protamine in function.

摘要

腺病毒主要核心蛋白VII的基因序列和相应蛋白质序列均已确定。该基因的确切位置在病毒基因组的43.37至44.90图谱坐标之间。蛋白VII长度为173个残基,分子量为19258。对其序列的详细分析揭示了由几个预测的α螺旋分隔的四个碱性结构域。有人提出,蛋白VII的链内折叠是由α螺旋的疏水相互作用驱动的,使该蛋白的碱性结构域与DNA磷酸相互作用。蛋白质单体可能在形成六聚体核小体样颗粒的过程中进一步相互结合。在宿主细胞的病毒感染周期中,蛋白VII的置换和替代似乎模拟了精子发生和受精过程中鱼精蛋白的生物学特性。尽管蛋白VII在功能上可能类似于鱼精蛋白,但鱼精蛋白样结构域的存在证实了其具有组蛋白/鱼精蛋白杂合分子结构。

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