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微生物蛋白中锚蛋白重复序列的功能多样性。

Functional diversity of ankyrin repeats in microbial proteins.

机构信息

Department of Microbiology and Immunology, College of Medicine, University of Louisville, Louisville, KY 40202, USA.

出版信息

Trends Microbiol. 2010 Mar;18(3):132-9. doi: 10.1016/j.tim.2009.11.004. Epub 2009 Dec 3.

Abstract

The ankyrin repeat (ANK) is the most common protein-protein interaction motif in nature, and is predominantly found in eukaryotic proteins. Genome sequencing of various pathogenic or symbiotic bacteria and eukaryotic viruses has identified numerous genes encoding ANK-containing proteins that are proposed to have been acquired from eukaryotes by horizontal gene transfer. However, the recent discovery of additional ANK-containing proteins encoded in the genomes of archaea and free-living bacteria suggests either a more ancient origin of the ANK motif or multiple convergent evolution events. Many bacterial pathogens employ various types of secretion systems to deliver ANK-containing proteins into eukaryotic cells, where they mimic or manipulate various host functions. Studying the molecular and biochemical functions of this family of proteins will enhance our understanding of important host-microbe interactions.

摘要

锚定重复(ANK)是自然界中最常见的蛋白质-蛋白质相互作用基序,主要存在于真核蛋白中。对各种致病性或共生细菌和真核病毒的基因组测序已经鉴定出许多编码含有ANK 的蛋白质的基因,这些基因被认为是通过水平基因转移从真核生物中获得的。然而,最近在古菌和自由生活细菌的基因组中发现了额外的含有ANK 的蛋白质编码,这表明 ANK 基序的起源更早,或者发生了多次趋同进化事件。许多细菌病原体利用各种类型的分泌系统将含有ANK 的蛋白质输送到真核细胞中,在真核细胞中,它们模拟或操纵各种宿主功能。研究这一家族蛋白质的分子和生化功能将增强我们对重要的宿主-微生物相互作用的理解。

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