Comparison of the EBNA1 proteins of Epstein-Barr virus and herpesvirus papio in sequence and function.
Comparison of the EBNA1 proteins of Epstein-Barr virus and herpesvirus papio in sequence and function.
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EB病毒和狒狒疱疹病毒的EBNA1蛋白序列和功能比较。
DOI：
10.1006/viro.1996.0392
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Ying,A
中科院分区：
文献类型：
--
作者：
Yates,JL;Camiolo,SM;Ali,S;Ying,A
EB病毒（EBV）的EBNA 1蛋白支持在潜伏感染的细胞中复制和维持环状病毒染色体。我们已经分离，测序和功能特征的EBNA 1基因的疱疹病毒乳头瘤病毒（HVP），一种EBV样病毒感染狒狒。如果在计算中省略含甘氨酸和丙氨酸的重复区的长度差异，则HVP和EBV的EBNA 1的氨基酸序列是56%相同的，其中含甘氨酸和丙氨酸的重复区的长度对于HVP EBNA 1短得多。DNA结合/二聚化结构域（羧基末端结构域）的关键结构特征似乎是保守的，因为这两个区域中的氨基酸被认为对DNA结合最关键。EBNA 1的氨基末端三分之二（氨基末端结构域）的大多数显著特征，包括缺乏预测α-螺旋或β-折叠结构的序列，由这两个序列共享，尽管该区域中的许多缺口需要用于序列的比对。EB病毒和HVP的EBNA 1的氨基端50个氨基酸弱类似于大鼠核糖体蛋白S2的氨基端。携带任一病毒的质粒载体在哺乳动物细胞中稳定复制，并且当被来自任一病毒的EBNA 1支持时，支持在选择下的集落的有效生长，尽管对于每种质粒载体，存在对来自相同病毒的EBNA 1的明显偏好。HVP EBNA 1在激活EBVoriP的增强子功能方面不如EBV EBNA 1有效，并且在某些条件下在支持携带EBVoriP的质粒的维持方面不如EBV EBNA 1有效。用杂交EBNA 1分子获得的结果表明，氨基末端和羧基末端结构域的差异分别是分别导致转录激活和质粒维持差异的主要原因。结果表明，EBNA 1内的变化可以差异地改变其转录和复制活性。
The EBNA1 protein of Epstein–Barr virus (EBV) supports replication and maintenance of the circularized viral chromosome in cells that are latently infected. We have isolated, sequenced, and functionally characterized the EBNA1 gene of herpesvirus papio (HVP), an EBV-like virus that infects baboons. The amino acid sequences of EBNA1 of HVP and EBV are 56% identical, if the difference in the length of the glycine and alanine containing repetitive region, which is much shorter for HVP EBNA1, is omitted for the calculation. The key structural features of the DNA-binding/dimerization domain (the carboxyl-terminal domain) appear to have been conserved, as have amino acids in the two regions thought to be most critical for DNA binding. Most of the salient features of the amino-terminal two-thirds of EBNA1 (the amino-terminal domain), including a dearth of sequences predictive of alpha-helical or beta-sheet structures, are shared by the two sequences, although numerous gaps in this region were needed for alignment of the sequences. The amino-terminal fifty amino acids of EBNA1 of both EBV and HVP weakly resemble the amino terminus of rat ribosomal protein S2. Plasmids carryingoriPof either virus replicated stably in mammalian cells and supported efficient outgrowth of colonies under selection when supported by EBNA1 from either virus, although with eachoriPthere was a noticeable preference for EBNA1 to be from the same virus. HVP EBNA1 was less effective than EBV EBNA1 at activating the enhancer function of EBVoriPand under certain conditions was less effective than EBV EBNA1 at supporting maintenance of plasmids carrying EBVoriP.Results obtained with hybrid EBNA1 molecules indicated that differences in the amino-terminal and carboxyl-terminal domains, respectively, are primarily responsible for the differences in transcriptional activation and plasmid maintenance, respectively. The results showed that changes within EBNA1 can differentially alter its transcriptional and replicational activities.