来自卡氏肺孢子虫的一个与真菌H⁺ATP酶极为相似的ATP酶基因的克隆与特性分析

Cloning and characterization of an ATPase gene from Pneumocystis carinii which closely resembles fungal H+ ATPases.

作者信息

Meade J C, Stringer J R

机构信息

Department of Microbiology, University of Mississippi Medical Center, Jackson 39216-4505, USA.

出版信息

J Eukaryot Microbiol. 1995 May-Jun;42(3):298-307. doi: 10.1111/j.1550-7408.1995.tb01584.x.

DOI:10.1111/j.1550-7408.1995.tb01584.x

PMID:7496388

Abstract

A gene encoding a P-type cation translocating ATPase was cloned from a genomic library of rat-derived Pneumocystis carinii. The nucleotide sequence of the gene contains a 2781 base-pair open reading frame that is predicted to encode a 101,401 dalton protein composed of 927 amino acids. The P. carinii ATPase protein (pcal) is 69-75% identical when compared with eight proton pumps from six fungal species. The Pneumocystis ATPase is less than 34% identical to ATPase proteins from protozoans, vertebrates or the Ca++ ATPases of yeast. The P. carinii ATPase contains 115 of 121 residues previously identified as characteristic of H+ ATPases. Alignment of the Pneumocystis and fungal proton pumps reveals five homologous domains specific for fungal H+ ATPases.

摘要

从大鼠源性卡氏肺孢子虫的基因组文库中克隆出一个编码P型阳离子转运ATP酶的基因。该基因的核苷酸序列包含一个2781个碱基对的开放阅读框，预计可编码一个由927个氨基酸组成、分子量为101,401道尔顿的蛋白质。与来自6种真菌的8种质子泵相比，卡氏肺孢子虫ATP酶蛋白（pcal）的同源性为69%-75%。肺孢子虫ATP酶与原生动物、脊椎动物的ATP酶或酵母的Ca++ ATP酶的同源性小于34%。卡氏肺孢子虫ATP酶含有121个先前确定为H+ ATP酶特征的残基中的115个。肺孢子虫和真菌质子泵的比对揭示了真菌H+ ATP酶特有的五个同源结构域。