Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes.
Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes.
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DOI：
10.1186/1471-2164-6-129
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发表时间：
2005-09-19
期刊：
影响因子：
4.4
通讯作者：
Srinivasan N
中科院分区：
文献类型：
--
作者：
Krupa A;Srinivasan N
Ser/Thr/Tyr激酶（STYKs）在真核生物中普遍存在，近年来在许多细菌中发现。最近的研究阐明了它们的细胞功能，确定了它们在细菌生长和发育中的作用。然而，大量细菌STYKs的功能仍然是难以捉摸的。在一个大的数据集的细菌STYKs的结构域的组织已在这里进行了研究，以识别各种结构域组合，确定细菌STYKs的功能。使用敏感的序列和配置文件搜索方法，结构域组织超过600 STYKs从125个原核基因组已被检查。已经鉴定了STYK的激酶催化结构域与广泛的酶结构域如磷酸酶、HSP 70、肽基脯氨酰异构酶、果胶酯酶和糖蛋白酶连接。这种对结构域组合的独特偏好不存在于组氨酸激酶或真核STYK家族中。在当前的分析中也注意到特定于某些细菌组的STYK的结构域组织。例如，分枝杆菌STYK中的疏水蛋白样结构域和革兰氏阳性生物的少数STYK中的青霉素结合结构域以及蓝藻STYK中的FHA结构域。原核STYK的特征性底物的同源物也已被鉴定。所鉴定的大多数细菌STYKs的结构域和结构域架构与真核生物STYKs中已知的结构域组织非常不同。这一观察结果突出了细菌STYKs与真核STYKs相比的独特生物学作用。细菌STYKs揭示了结构域组织的高度多样性。一些在不同细菌物种中保守的模块化组织表明它们在细菌生理学中的核心作用。独特的结构域架构的几个其他组的STYKs揭示招聘特定的物种的功能。
Ser/Thr/Tyr kinases (STYKs) commonly found in eukaryotes have been recently reported in many bacterial species. Recent studies elucidating their cellular functions have established their roles in bacterial growth and development. However functions of a large number of bacterial STYKs still remain elusive. The organisation of domains in a large dataset of bacterial STYKs has been investigated here in order to recognise variety in domain combinations which determine functions of bacterial STYKs. Using sensitive sequence and profile search methods, domain organisation of over 600 STYKs from 125 prokaryotic genomes have been examined. Kinase catalytic domains of STYKs tethered to a wide range of enzymatic domains such as phosphatases, HSP70, peptidyl prolyl isomerases, pectin esterases and glycoproteases have been identified. Such distinct preferences for domain combinations are not known to be present in either the Histidine kinase or the eukaryotic STYK families. Domain organisation of STYKs specific to certain groups of bacteria has also been noted in the current anlaysis. For example, Hydrophobin like domains in Mycobacterial STYK and penicillin binding domains in few STYKs of Gram-positive organisms and FHA domains in cyanobacterial STYKs. Homologues of characterised substrates of prokaryotic STYKs have also been identified. The domains and domain architectures of most of the bacterial STYKs identified are very different from the known domain organisation in STYKs of eukaryotes. This observation highlights distinct biological roles of bacterial STYKs compared to eukaryotic STYKs. Bacterial STYKs reveal high diversity in domain organisation. Some of the modular organisations conserved across diverse bacterial species suggests their central role in bacterial physiology. Unique domain architectures of few other groups of STYKs reveal recruitment of functions specific to the species.
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