Vayda M E, Rogers A E, Flint S J
Nucleic Acids Res. 1983 Jan 25;11(2):441-60. doi: 10.1093/nar/11.2.441.
The morphology, protein composition and DNA organization of nucleoprotein core complexes isolated from type 5 adenovirions have been examined by electron microscopy and biochemical techniques. The morphology of such core structures is in some ways strikingly similar to that exhibited by cellular chromatin. 'Native' core preparations contain compact and less highly-folded forms: the latter appear as thick fibres, 150-300A in diameter. Upon exposure to 0.4M NaCl, adenovirus cores undergo a transition to a beaded string form, reminiscent of nucleosomes. Of the three arginine-rich proteins, polypeptides V, VII and mu present in 'native' cores, only polypeptide VII remains associated with viral DNA in the presence of 0.4M NaCl. We therefore conclude that the nucleosome-like beads are constructed solely of polypeptide VII. The results of micrococcal nuclease digestion experiments suggest that polypeptide VII is sufficient to protect some 100-300bp of adenoviral DNA.
已通过电子显微镜和生化技术对从5型腺病毒颗粒中分离出的核蛋白核心复合物的形态、蛋白质组成和DNA组织进行了研究。此类核心结构的形态在某些方面与细胞染色质的形态惊人地相似。“天然”核心制剂包含紧密且折叠程度较低的形式：后者表现为直径150 - 300埃的粗纤维。暴露于0.4M NaCl后，腺病毒核心转变为串珠状，类似于核小体。在“天然”核心中存在的三种富含精氨酸的蛋白质，即多肽V、VII和μ中，在0.4M NaCl存在的情况下，只有多肽VII仍与病毒DNA结合。因此我们得出结论，核小体样珠子仅由多肽VII构成。微球菌核酸酶消化实验结果表明，多肽VII足以保护约100 - 300bp的腺病毒DNA。
