Amikam Dorit, Galperin Michael Y
Department of Biotechnology and Environmental Sciences, Tel-Hai Academic College Tel-Hai, Israel.
Bioinformatics. 2006 Jan 1;22(1):3-6. doi: 10.1093/bioinformatics/bti739. Epub 2005 Oct 25.
Recent studies identified c-di-GMP as a universal bacterial secondary messenger regulating biofilm formation, motility, production of extracellular polysaccharide and multicellular behavior in diverse bacteria. However, except for cellulose synthase, no protein has been shown to bind c-di-GMP and the targets for c-di-GMP action remain unknown. Here we report identification of the PilZ ("pills") domain (Pfam domain PF07238) in the sequences of bacterial cellulose synthases, alginate biosynthesis protein Alg44, proteins of enterobacterial YcgR and firmicute YpfA families, and other proteins encoded in bacterial genomes and present evidence indicating that this domain is (part of) the long-sought c-di-GMP-binding protein. Association of the PilZ domain with a variety of other domains, including likely components of bacterial multidrug secretion system, could provide clues to multiple functions of the c-di-GMP in bacterial pathogenesis and cell development.
最近的研究确定环二鸟苷酸（c-di-GMP）是一种通用的细菌第二信使，可调节多种细菌中的生物膜形成、运动性、细胞外多糖的产生和多细胞行为。然而，除了纤维素合酶外，尚未发现有蛋白质能与c-di-GMP结合，c-di-GMP的作用靶点仍然未知。在此，我们报告在细菌纤维素合酶、藻酸盐生物合成蛋白Alg44、肠杆菌YcgR家族和厚壁菌YpfA家族的蛋白质以及细菌基因组中编码的其他蛋白质序列中鉴定出PilZ（“菌毛”）结构域（Pfam结构域PF07238），并提供证据表明该结构域是长期以来寻找的c-di-GMP结合蛋白（的一部分）。PilZ结构域与多种其他结构域的关联，包括可能的细菌多药分泌系统的组成部分，可能为c-di-GMP在细菌发病机制和细胞发育中的多种功能提供线索。
