Department of Biology, University of Alabama at Birmingham, AL 35294-1170, USA.
FEMS Microbiol Lett. 2011 Jun;319(2):106-14. doi: 10.1111/j.1574-6968.2011.02269.x. Epub 2011 Apr 18.
A cold shock domain (CSD)-containing protein, CspD, of molecular mass ~7.28 kDa in a psychrotolerant Antarctic Janthinobacterium sp. Ant5-2 (ATCC BAA-2154) exhibited constitutive expression at 37, 22, 15, 4 and -1°C. The cspD gene encoding the CspD protein of Ant5-2 was cloned, sequenced and analyzed. The deduced protein sequence was highly similar to the conserved domains of the cold shock proteins (Csps) from bacteria belonging to the class Betaproteobacteria. Its expression was both time- and growth phase-dependent and increased when exposed to 37°C and UV radiation (UVC, dose: 1.8 and 2.8 mJ cm(-2)). The results from the electrophoretic mobility shift and subcellular localization study confirmed its single-stranded DNA-binding property. In silico analysis of the deduced tertiary structure of CspD from Ant5-2 showed a highly stable domain-swapped dimer, forming two similar monomeric Csp folds. This study established an overall framework of the structure, function and phylogenetic analysis of CspD from an Antarctic Janthinobacterium sp. Ant5-2, which may facilitate and stimulate the study of CSD fold proteins in the class Betaproteobacteria.
一种冷休克结构域（CSD）包含的蛋白质，CspD，在耐冷的南极 Janthinobacterium sp. Ant5-2（ATCC BAA-2154）中，分子量约为 7.28 kDa，在 37°C、22°C、15°C、4°C 和-1°C 时均为组成型表达。Ant5-2 中编码 CspD 蛋白的 cspD 基因被克隆、测序和分析。推导的蛋白质序列与属于β变形菌纲的细菌的冷休克蛋白（Csps）的保守结构域高度相似。其表达既依赖于时间又依赖于生长阶段，当暴露于 37°C 和紫外线辐射（UVC，剂量：1.8 和 2.8 mJ cm(-2)) 时，其表达增加。电泳迁移率变动和亚细胞定位研究的结果证实了其单链 DNA 结合特性。来自 Ant5-2 的 CspD 的推导出的三级结构的计算分析表明高度稳定的结构域交换二聚体，形成两个类似的单体 Csp 折叠。这项研究建立了来自南极 Janthinobacterium sp. Ant5-2 的 CspD 的结构、功能和系统发育分析的整体框架，这可能有助于并刺激β变形菌纲中 CSD 折叠蛋白的研究。
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