Berna Anne, Scott Ken, Chabrière Eric, Bernier François
Institut de Biologie Moléculaire des Plantes du CNRS, Université Louis Pasteur, Institut de Botanique, Strasbourg Cedex, France.
Bioessays. 2009 May;31(5):570-80. doi: 10.1002/bies.200800174.
PstS and DING proteins are members of a superfamily of secreted, high-affinity phosphate-binding proteins. Whereas microbial PstS have a well-defined role in phosphate ABC transporters, the physiological function of DING proteins, named after their DINGGG N termini, still needs to be determined. PstS and DING proteins co-exist in some Pseudomonas strains, to which they confer a highly adhesive and virulent phenotype. More than 30 DING proteins have now been purified, mostly from eukaryotes. They are often associated with infections or with dysregulation of cell proliferation. Consequently, eukaryotic DING proteins could also be involved in cell-cell communication or adherence. The ubiquitous presence in eukaryotes of proteins structurally and functionally related to bacterial virulence factors is intriguing, as is the absence of eukaryotic genes encoding DING proteins in databases. DING proteins in eukaryotes could originate from unidentified commensal or symbiotic bacteria and could contribute to essential functions. Alternatively, DING proteins could be encoded by eukaryotic genes sharing special features that prevent their cloning. Both hypotheses are discussed.
PstS蛋白和DING蛋白是分泌型高亲和力磷酸盐结合蛋白超家族的成员。微生物PstS蛋白在磷酸盐ABC转运蛋白中具有明确的作用,而DING蛋白(因其DINGGG N端而得名)的生理功能仍有待确定。PstS蛋白和DING蛋白在一些假单胞菌菌株中共存,赋予这些菌株高度黏附性和毒性表型。目前已纯化出30多种DING蛋白,其中大部分来自真核生物。它们常与感染或细胞增殖失调有关。因此,真核生物的DING蛋白也可能参与细胞间通讯或黏附。真核生物中存在与细菌毒力因子在结构和功能上相关的蛋白,这很有趣,同时数据库中缺乏编码DING蛋白的真核基因也很有意思。真核生物中的DING蛋白可能起源于未鉴定的共生或共生细菌,并可能有助于基本功能。或者,DING蛋白可能由具有特殊特征而阻止其克隆的真核基因编码。本文对这两种假设都进行了讨论。