Vos H L, van der Lee F M, Reemst A M, van Loon A E, Sussenbach J S
Laboratory of Physiological Chemistry, State University of Utrecht, the Netherlands.
Virology. 1988 Mar;163(1):1-10. doi: 10.1016/0042-6822(88)90227-9.
The adenovirus (Ad) single-stranded DNA binding protein (DBP) is a multifunctional protein. It is thought to consist of two domains, the amino-terminal domain involved in host-range determination and the carboxyl-terminal domain functioning in DNA replication and DNA binding. We have determined the nucleotide sequences of the DBP genes of Ad40 and Ad41, two human adenoviral serotypes that differ significantly from other adenoviruses. Regions of structural and functional importance in the corresponding proteins could be identified by comparison of the amino acid sequences with those of other known DBPs. In addition, the nucleotide sequences of the DBP early promoters, of the 23K protease genes, and of parts of the hexon and 100K protein genes have been determined. It can be deduced from the nucleotide sequences, that the Ad40 and Ad41 DBPs are relatively small (473 and 474 amino acids (a.a.), respectively, versus 529 a.a. for the Ad5 DBP). This is caused by the presence of very small amino-terminal domains of 119 a.a. (Ad40) and 120 a.a. (Ad41), as compared to 173 a.a. for the corresponding Ad5 domain. Only a few amino acids in this domain have been conserved in all known DBPs. The carboxyl-terminal domains show a higher degree of sequence conservation. In this domain, four strongly conserved regions can be identified, one of which might form a metal-binding site. The 23K proteases of both Ad40 and Ad41 show a strong homology to the Ad2 and Ad5 proteins, with the exception of the carboxyl-terminal end of the proteins. The 23K protease gene of Ad41 has an open reading frame that extends beyond the polyadenylation signal, in contrast to the Ad40 gene that ends well in front of the signal.
腺病毒（Ad）单链DNA结合蛋白（DBP）是一种多功能蛋白。它被认为由两个结构域组成，即参与宿主范围确定的氨基末端结构域和在DNA复制及DNA结合中起作用的羧基末端结构域。我们已经确定了Ad40和Ad41的DBP基因的核苷酸序列，这两种人类腺病毒血清型与其他腺病毒有显著差异。通过将相应蛋白质的氨基酸序列与其他已知DBP的序列进行比较，可以确定其结构和功能重要区域。此外，还确定了DBP早期启动子、23K蛋白酶基因以及六邻体和100K蛋白基因部分的核苷酸序列。从核苷酸序列可以推断，Ad40和Ad41的DBP相对较小（分别为473和474个氨基酸，而Ad5的DBP为529个氨基酸）。这是由于存在非常小的氨基末端结构域，Ad40为119个氨基酸，Ad41为120个氨基酸，而相应的Ad5结构域为173个氨基酸。在所有已知的DBP中，该结构域仅保留了少数几个氨基酸。羧基末端结构域显示出更高程度的序列保守性。在该结构域中，可以识别出四个高度保守的区域，其中一个可能形成金属结合位点。Ad40和Ad41的23K蛋白酶与Ad2和Ad5的蛋白具有很强的同源性，但蛋白质的羧基末端除外。Ad41的23K蛋白酶基因有一个开放阅读框，延伸到多聚腺苷酸化信号之外，而Ad40基因在该信号之前就很好地结束了。
