Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, P.R. China.
Metallomics. 2013 Oct;5(10):1423-9. doi: 10.1039/c3mt00059a.
Increasing amounts of histidine-rich proteins (HRPs) have been found in microorganisms. We systematically analyzed the proteomes of 675 prokaryotes including 52 archaea and 623 bacteria for histidine-rich motifs (HRMs). We show that HRPs are widespread in prokaryotic proteomes, with the majority being involved in metal homeostasis. HRPs are frequently found in the proteomes of certain orders of rhizobia and pathogenic Gram-negative bacteria, but are essentially absent in obligate intracellular pathogenic species. The occurrence of HRPs in the proteomes of prokaryotes is related to their habitats. We further revealed a class of globally histidine-rich bacterial proteins. This approach can readily be used to identify other single amino acid rich motifs (and proteins) in microbial proteomes to facilitate the exploration of their functions.
越来越多的富含组氨酸的蛋白质（HRPs）已在微生物中被发现。我们系统地分析了包括 52 种古菌和 623 种细菌在内的 675 种原核生物的蛋白质组中的富含组氨酸基序（HRMs）。结果表明，HRPs 在原核生物蛋白质组中广泛存在，其中大多数与金属稳态有关。HRPs 经常在根瘤菌和某些致病性革兰氏阴性菌的蛋白质组中被发现，但在专性细胞内致病性物种中基本不存在。HRPs 在原核生物蛋白质组中的出现与其栖息地有关。我们进一步揭示了一类在全球范围内富含组氨酸的细菌蛋白。这种方法可以很容易地用于鉴定微生物蛋白质组中的其他单一氨基酸丰富基序（和蛋白质），以促进对其功能的探索。
