The evolution of an osmotically inducible dps in the genus Streptomyces.

The evolution of an osmotically inducible dps in the genus Streptomyces.
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DOI:
10.1371/journal.pone.0060772
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发表时间:
2013
期刊:
影响因子:
3.7
通讯作者:
Del Sol R
Del Sol R
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Facey PD;Hitchings MD;Williams JS;Skibinski DO;Dyson PJ;Del Sol R

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Dps 蛋白几乎普遍存在于细菌基因组中,现在人们认识到它们在各种应激反应中的多方面作用。先前的研究表明,该蛋白质家族组装成十二聚体,其四级结构对其功能至关重要。此外,每个细菌基因组的 dps 基因数量是可变的;即使在密切相关的物种中 - 然而,对于许多属来说,这个谜团尚未得到令人满意的解释。我们重建了链霉菌基因组中 Dps 最可能的进化历史。通常,这些细菌编码不止一种 Dps 蛋白。我们提供的解释是,紧密相关的链霉菌中每个基因组 dps 数量的变化可以通过基因重复或横向获取来解释,而前者先于所得旁系同源物之一的表达模式的后续转变。我们发现天蓝色链球菌的基因组编码三种 Dps 蛋白,其中包括无尾 Dps。我们的体内观察表明,与天蓝色链球菌中的其他两种 DPS 不同,无尾蛋白不易寡聚。系统发育和生物信息学分析与表达研究相结合表明,在几种链霉菌属物种中,至少一种 Dps 在渗透压休克过程中显着过度表达,但直系同源物的身份有所不同。 dps 启动子区域的计算机分析与重复 dps 基因的基因表达研究相结合表明,旁系同源基因对表达差异,这与 sigB 启动子的存在相关。最后,我们鉴定了一个罕见的新型 Dps 进化枝,并表明天蓝色链球菌中这些蛋白质的代表具有高稳定性的十二聚四级结构。
Dps proteins are found almost ubiquitously in bacterial genomes and there is now an appreciation of their multifaceted roles in various stress responses. Previous studies have shown that this family of proteins assemble into dodecamers and their quaternary structure is entirely critical to their function. Moreover, the numbers of dps genes per bacterial genome is variable; even amongst closely related species - however, for many genera this enigma is yet to be satisfactorily explained. We reconstruct the most probable evolutionary history of Dps in Streptomyces genomes. Typically, these bacteria encode for more than one Dps protein. We offer the explanation that variation in the number of dps per genome among closely related Streptomyces can be explained by gene duplication or lateral acquisition, and the former preceded a subsequent shift in expression patterns for one of the resultant paralogs. We show that the genome of S. coelicolor encodes for three Dps proteins including a tailless Dps. Our in vivo observations show that the tailless protein, unlike the other two Dps in S. coelicolor, does not readily oligomerise. Phylogenetic and bioinformatic analyses combined with expression studies indicate that in several Streptomyces species at least one Dps is significantly over-expressed during osmotic shock, but the identity of the ortholog varies. In silico analysis of dps promoter regions coupled with gene expression studies of duplicated dps genes shows that paralogous gene pairs are expressed differentially and this correlates with the presence of a sigB promoter. Lastly, we identify a rare novel clade of Dps and show that a representative of these proteins in S. coelicolor possesses a dodecameric quaternary structure of high stability.
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期刊: PROTEIN ENGINEERING
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