Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella livingstonensis Ac10, for global identification of cold-inducible proteins
Proteomic studies of an Antarctic cold-adapted bacterium, Shewanella livingstonensis Ac10, for global identification of cold-inducible proteins
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DOI：
10.1007/s00792-007-0098-6
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发表时间：
2007-11-01
期刊：
影响因子：
2.9
通讯作者：
Esaki, Nobuyoshi
中科院分区：
文献类型：
--
作者：
Kawamoto, Jun;Kurihara, Tatsuo;Esaki, Nobuyoshi
对从南极海水中分离到的一株冷适应细菌Shewanella livingstonensis Ac 10进行了蛋白质组学分析，以阐明其冷适应机制。细胞在4 ℃和18 ℃下生长，通过二维凝胶电泳分析可溶性和膜蛋白。在4 ℃时，47种可溶性蛋白和5种膜蛋白的相对丰度增加了两倍以上，并通过肽质量指纹图谱分析了这些蛋白。鉴定了26种可溶性蛋白和2种膜蛋白。这些蛋白质包括参与RNA合成和折叠（RpoA、GreA和CspA）、蛋白质合成和折叠（TufB、Efp、LysU和Tig）、膜转运（OmpA和OmpC）和运动性（FlgE和FlgL）的蛋白质。冷诱导的RpoA、GreA和CspA可能是在低温下RNA的有效和准确转录和正确折叠所需要的，其中核酸的碱基配对是稳定的，并且倾向于形成不期望的RNA二级结构。Tig被认为具有肽基-脯氨酰顺反异构酶活性，并促进蛋白质在低温下的正确折叠。OmpA和OmpC的冷诱导可能会抵消低温下溶质的低扩散速率，并使营养物质的有效吸收成为可能。这些结果为了解微生物的冷适应机制提供了许多线索。
Proteomic analysis of a cold-adapted bacterium, Shewanella livingstonensis Ac10, isolated from Antarctic seawater was carried out to elucidate its coldadaptation mechanism. The cells were grown at 4 degrees C and 18 degrees C, and soluble and membrane proteins were analyzed by two-dimensional gel electrophoresis. At 4 degrees C, the relative abundance of 47 soluble proteins and five membrane proteins increased more than twofold, and these proteins were analyzed by peptide mass fingerprinting. Twenty-six soluble proteins and two membrane proteins were identified. These included proteins involved in RNA synthesis and folding (RpoA, GreA, and CspA), protein synthesis and folding (TufB, Efp, LysU, and Tig), membrane transport (OmpA and OmpC), and motility (FlgE and FlgL). Cold-inducible RpoA, GreA, and CspA may be required for efficient and accurate transcription and proper folding of RNA at low temperatures, where base pairing of nucleic acids is stable and undesired secondary structures of RNA tend to form. Tig is supposed to have peptidyl-prolyl cis-trans isomerase activity and facilitate proper folding of proteins at low temperatures. The cold induction of OmpA and OmpC is likely to counteract the low diffusion rate of solutes at low temperatures and enables the efficient uptake of nutrients. These results provided many clues to understand microbial cold-adaptation mechanisms.