Hammond J M, Kerr S M, Smith G L, Dixon L K
AFRC Institute for Animal Health, Pirbright Laboratory, Woking, Surrey, UK.
Nucleic Acids Res. 1992 Jun 11;20(11):2667-71. doi: 10.1093/nar/20.11.2667.
Sequence analysis of the SalI g region of the genome of a virulent isolate of ASFV (Malawi Lil 20/1) has revealed an open reading frame with the potential to encode a 48 kilodalton (kD) polypeptide which has significant homology with eukaryotic and prokaryotic DNA ligases. This ASFV encoded gene also contains the putative active site region of DNA ligases including the lysine residue which is necessary for enzyme-adenylate adduct formation, but lacks the C-terminal basic region conserved in other eukaryotic DNA ligases. A novel [32P]-labelled potential DNA ligase-adenylate adduct of M(r) 45 kD was observed upon incubation of ASFV infected cell cytoplasmic extracts with alpha-[32P]-ATP and subsequent analysis of products by SDS/PAGE. These data together suggest that ASFV encodes its own DNA ligase.
对非洲猪瘟病毒（ASFV）强毒株（马拉维 Lil 20/1）基因组的 SalI g 区域进行序列分析，发现了一个开放阅读框，它有可能编码一种 48 千道尔顿（kD）的多肽，该多肽与真核生物和原核生物的 DNA 连接酶具有显著的同源性。这个 ASFV 编码基因还包含 DNA 连接酶的假定活性位点区域，包括酶 - 腺苷酸加合物形成所必需的赖氨酸残基，但缺乏其他真核生物 DNA 连接酶中保守的 C 末端碱性区域。在用α-[32P]-ATP 孵育 ASFV 感染细胞的细胞质提取物并随后通过 SDS/PAGE 分析产物时，观察到了一种新的分子量为 45 kD 的[32P]标记的潜在 DNA 连接酶 - 腺苷酸加合物。这些数据共同表明 ASFV 编码其自身的 DNA 连接酶。
