古核生物 GINS 蛋白与古菌的引物酶催化亚基 PriS 具有共同的结构域。
The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain.
机构信息
Centre for Biomolecular Sciences, School of Biology, University of St Andrews, North Haugh, St Andrews, Fife KY16 9ST, UK.
出版信息
Biol Direct. 2010 Apr 12;5:17. doi: 10.1186/1745-6150-5-17.
UNLABELLED
Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B-domains of the archaeo-eukaryotic GINS proteins in the form of a conserved structural domain comprising a three-stranded antiparallel beta-sheet adjacent to an alpha-helix and a two-stranded beta-sheet or hairpin. The presence of a shared domain in archaeal PriS and GINS proteins, the genes for which are often found adjacent on the chromosome, suggests simple mechanisms for the evolution of these proteins.
REVIEWERS
This article was reviewed by Zvi Kelman (nominated by Michael Galperin) and Kira Makarova.
未加标签
原酶和 GINS 是真核细胞和古细菌中染色体 DNA 复制的必需因素。在这里，我们描述了以前未被发现的古细菌原酶的催化亚基（PriS）的 C 末端结构域与古细菌真核 GINS 蛋白的 B 结构域之间的关系，这种关系以包含三个反向平行β-折叠的保守结构域的形式存在，与一个α-螺旋相邻，还有两个反向平行β-折叠或发夹。古细菌 PriS 和 GINS 蛋白中存在共享结构域，这些基因通常在染色体上相邻，这表明了这些蛋白进化的简单机制。
审稿人
本文由 Zvi Kelman（由 Michael Galperin 提名）和 Kira Makarova 进行了评审。
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