The angiotensin-converting enzyme (ACE) gene family of Anopheles gambiae.

The angiotensin-converting enzyme (ACE) gene family of Anopheles gambiae.
复制标题

血管紧张素转换酶(ACE)基因gambiae的基因家族。

DOI:
10.1186/1471-2164-6-172
复制
发表时间:
2005-12-05
期刊:
影响因子:
4.4
通讯作者:
Shirras, Alan D
Shirras, Alan D
中科院分区:
生物学2区
文献类型:
--
作者:
Burnham, Susan;Smith, Judith A;Lee, Alison J;Isaac, R Elwyn;Shirras, Alan D

文献摘要

被引文献

相似文献

M2多肽酶家族成员与哺乳动物血管紧张素转换酶(ACE)相关,在调节多种生理过程中发挥重要作用。随着越来越多的无脊椎动物基因组被测序,越来越多的证据表明M2多肽酶基因多种多样,甚至在单个物种中也是如此。这些血管紧张素转换酶类似蛋白的功能在很大程度上是未知的。冈比亚按蚊基因组测序发现了一些类似ACE的基因,但EnSembl注释中可能存在的错误使得类似ACE的基因的数量及其结构尚不清楚。TBLASTN和cDNA序列分析表明,冈比亚按蚊基因组包含9个基因(AnoACE基因),它们编码与哺乳动物ACE相似的蛋白质。这些基因中有8个编码可能的单域酶,类似于到目前为止描述的其他昆虫王牌。然而,AnoACE9具有哺乳动物体细胞ACE的几个共同特征,如双结构域结构和疏水C末端。4个AnoACE基因(2、3、7和9)在不同的发育阶段都有表达。AnoACE3、AnoACE7和AnoACE9的表达是由血粉诱导的,其中AnoACE7的诱导作用最大(约10倍)。在进化过程中,编码两个结构域的ACEs的基因已经出现了几次,这表明在一个蛋白质中拥有一个具有两个活性位点的ACE具有共同的选择优势。AnoACE7属于昆虫ACEs的一个亚类,很可能是膜结合的,具有不寻常的保守基因结构。
Members of the M2 family of peptidases, related to mammalian angiotensin converting enzyme (ACE), play important roles in regulating a number of physiological processes. As more invertebrate genomes are sequenced, there is increasing evidence of a variety of M2 peptidase genes, even within a single species. The function of these ACE-like proteins is largely unknown. Sequencing of the A. gambiae genome has revealed a number of ACE-like genes but probable errors in the Ensembl annotation have left the number of ACE-like genes, and their structure, unclear. TBLASTN and sequence analysis of cDNAs revealed that the A. gambiae genome contains nine genes (AnoACE genes) which code for proteins with similarity to mammalian ACE. Eight of these genes code for putative single domain enzymes similar to other insect ACEs described so far. AnoACE9, however, has several features in common with mammalian somatic ACE such as a two domain structure and a hydrophobic C terminus. Four of the AnoACE genes (2, 3, 7 and 9) were shown to be expressed at a variety of developmental stages. Expression of AnoACE3, AnoACE7 and AnoACE9 is induced by a blood meal, with AnoACE7 showing the largest (approximately 10-fold) induction. Genes coding for two-domain ACEs have arisen several times during the course of evolution suggesting a common selective advantage to having an ACE with two active-sites in tandem in a single protein. AnoACE7 belongs to a sub-group of insect ACEs which are likely to be membrane-bound and which have an unusual, conserved gene structure.