来自嗜热栖热菌的一种DNA聚合酶与B族DNA聚合酶存在序列相似性。
A DNA polymerase from the archaeon Sulfolobus solfataricus shows sequence similarity to family B DNA polymerases.
作者信息
Pisani F M, De Martino C, Rossi M
机构信息
Istituto di Biochimica delle Proteine ed Enzimologia, Consiglio Nazionale Ricerche, Naples, Italy.
出版信息
Nucleic Acids Res. 1992 Jun 11;20(11):2711-6. doi: 10.1093/nar/20.11.2711.
Abstract
The gene encoding the thermostable DNA polymerase from the archaeon Sulfolobus solfataricus (strain MT 4) was isolated by means of two degenerate oligonucleotide probes. They were designed on the basis of partial enzyme amino acid sequences. The gene was found to encode a 882 residues polypeptide chain with a deduced molecular mass of about 100 kDa. By comparison with other archaeal genes, putative regulatory sites were identified in the gene-flanking regions. By computer-assisted homology search, several sequence similarities among S. solfataricus and family B DNA polymerases were found. In addition, conserved sequence motifs, implicated in the 3'-5' exonuclease activity of E. coli DNA polymerase I and shared by various family A and B DNA polymerases, were also identified. This result suggests that the proofreading domains of all these enzymes are evolutionarily related.
摘要
利用两个简并寡核苷酸探针分离出嗜热栖热放线菌（菌株MT 4）中编码耐热DNA聚合酶的基因。它们是根据部分酶氨基酸序列设计的。该基因被发现编码一条由882个残基组成的多肽链，推导分子量约为100 kDa。通过与其他古细菌基因比较，在基因侧翼区域鉴定出假定的调控位点。通过计算机辅助同源性搜索，发现嗜热栖热放线菌与B族DNA聚合酶之间存在若干序列相似性。此外，还鉴定出了与大肠杆菌DNA聚合酶I的3'-5'核酸外切酶活性相关且为各种A族和B族DNA聚合酶所共有的保守序列基序。这一结果表明，所有这些酶的校对结构域在进化上是相关的。
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