A large family of eukaryotic-like protein Ser/Thr kinases of Myxococcus xanthus, a developmental bacterium.

S Inouye, R Jain, T Ueki, H Nariya, C Y Xu, M Y Hsu, B A Fernandez-Luque, J Munoz-Dorado, E Farez-Vidal, M Inouye
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引用次数: 50

Abstract

Myxococcus xanthus is a gram-negative bacterium that forms multicellular fruiting bodies upon starvation. Here, we demonstrate that it contains at least 13 eukaryotic-like protein Ser/Thr kinases (Pkn1 to Pkn13) individually having unique features. All contain the kinase domain of approximately 280 residues near the N-terminal end, which share highly conserved features in eukaryotic Ser/Thr kinases. The kinase domain is followed by a putative regulatory domain consisting of 185 to 692 residues. These regulatory domains share no significant sequence similarities. The C-terminal regions of 11 kinases contain at least 1 transmembrane domain, suggesting that they function as transmembrane sensor kinases. From the recent genomic analysis, protein Ser/Thr kinases were found in various pathogenic bacteria and coexist with protein His kinases. Phylogenetic analysis of these Ser/Thr kinases reveals that all bacterial Ser/Thr kinases were evolved from a common ancestral kinase together with eukaryotic Tyr and Ser/Thr kinases. Coexistence of both Ser/Thr and His kinases in some organisms may be significant in terms of functional differences between the two kinases. We argue that both kinases are essential for some bacteria to adapt optimally to severe environmental changes.

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黄粘球菌真核样蛋白丝氨酸/苏氨酸激酶大家族,一种发育性细菌
黄粘球菌是一种革兰氏阴性细菌,在饥饿时形成多细胞子实体。在这里,我们证明了它含有至少13个真核样蛋白丝氨酸/苏氨酸激酶(Pkn1至Pkn13),它们各自具有独特的特征。在真核丝氨酸/苏氨酸激酶中,它们都含有约280个靠近n端残基的激酶结构域,这些残基在真核丝氨酸/苏氨酸激酶中具有高度保守的特征。激酶结构域之后是一个由185到692个残基组成的推定调节结构域。这些调节结构域没有显著的序列相似性。11种激酶的c端至少包含1个跨膜结构域,表明它们具有跨膜传感器激酶的功能。从最近的基因组分析中发现,蛋白丝氨酸/苏氨酸激酶存在于多种致病菌中,并与蛋白His激酶共存。这些丝氨酸/苏氨酸激酶的系统发育分析表明,所有细菌丝氨酸/苏氨酸激酶都是与真核生物的酪氨酸和丝氨酸/苏氨酸激酶一起从一个共同的祖先激酶进化而来的。Ser/Thr和His激酶在某些生物体中共存,这两种激酶的功能差异可能是显著的。我们认为,这两种激酶对于一些细菌最优地适应严峻的环境变化是必不可少的。
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