FK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.
FK506-Binding protein 22 from a psychrophilic bacterium, a cold shock-inducible peptidyl prolyl isomerase with the ability to assist in protein folding.
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DOI：
10.3390/ijms12085261
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发表时间：
2011
影响因子：
5.6
通讯作者：
Kanaya S
中科院分区：
文献类型：
--
作者：
Budiman C;Koga Y;Takano K;Kanaya S
微生物对低温的适应仍有待充分阐明。肽基脯氨酰顺反异构酶（PPIases）参与了多种微生物的冷适应过程，无论是嗜热菌、中温菌还是嗜湿菌。在低温下顺反异构化的速率比在高温下慢得多，并且可能导致蛋白质折叠的问题。然而，PPIases参与冷适应的机制仍不清楚。在这里，我们使用FK 506结合蛋白22，一种来自嗜冷细菌希瓦氏菌属SIB 1（SIB 1 FKBP 22）的冷休克蛋白作为模型蛋白来破译PPIases参与冷适应。SIB 1 FKBP 22是同源二聚体，其基于三级模型呈现V形结构。每个单体由负责二聚化的N-结构域和C-催化结构域组成。SIB 1 FKBP 22是一种典型的冷适应酶，表现为在低温下催化效率的增加、最适活性温度的下移和构象稳定性的降低。SIB 1 FKBP 22被认为是折叠酶和伴侣，这是基于其分别催化含顺式脯氨酸的蛋白质的重折叠和结合折叠中间蛋白的能力。SIB 1 FKBP 22的折叠酶和伴侣蛋白活性被认为是希瓦氏菌SIB 1冷适应的重要因素。这些活性也被其他PPIases用于参与各种微生物的冷适应。尽管PPIases的其他生物学作用，我们提出PPIases的折叠酶和伴侣活性是克服微生物中由于蛋白质折叠引起的冷应激问题的主要要求。
Adaptation of microorganisms to low temperatures remains to be fully elucidated. It has been previously reported that peptidyl prolyl cis-trans isomerases (PPIases) are involved in cold adaptation of various microorganisms whether they are hyperthermophiles, mesophiles or phsycrophiles. The rate of cis-trans isomerization at low temperatures is much slower than that at higher temperatures and may cause problems in protein folding. However, the mechanisms by which PPIases are involved in cold adaptation remain unclear. Here we used FK506-binding protein 22, a cold shock protein from the psychrophilic bacterium Shewanella sp. SIB1 (SIB1 FKBP22) as a model protein to decipher the involvement of PPIases in cold adaptation. SIB1 FKBP22 is homodimer that assumes a V-shaped structure based on a tertiary model. Each monomer consists of an N-domain responsible for dimerization and a C-catalytic domain. SIB1 FKBP22 is a typical cold-adapted enzyme as indicated by the increase of catalytic efficiency at low temperatures, the downward shift in optimal temperature of activity and the reduction in the conformational stability. SIB1 FKBP22 is considered as foldase and chaperone based on its ability to catalyze refolding of a cis-proline containing protein and bind to a folding intermediate protein, respectively. The foldase and chaperone activites of SIB1 FKBP22 are thought to be important for cold adaptation of Shewanella sp. SIB1. These activities are also employed by other PPIases for being involved in cold adaptation of various microorganisms. Despite other biological roles of PPIases, we proposed that foldase and chaperone activities of PPIases are the main requirement for overcoming the cold-stress problem in microorganisms due to folding of proteins.
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影响因子：
5.6
作者：
ACHARYA, KR;STUART, DI;PHILLIPS, DC
通讯作者：
PHILLIPS, DC
DOI：
10.1073/pnas.95.19.11476
发表时间：
1998-09-15
影响因子：
11.1
作者：
Fields, PA;Somero, GN
通讯作者：
Somero, GN
影响因子：
11.4
作者：
HAYERHARTL, MK;EWBANK, JJ;HARTL, FU
通讯作者：
HARTL, FU
影响因子：
5.4
作者：
Budiman, Cahyo;Bando, Keisuke;Kanaya, Shigenori
通讯作者：
Kanaya, Shigenori
影响因子：
2.9
作者：
Hu, Kaifeng;Galius, Veniamin;Pervushin, Konstantin
通讯作者：
Pervushin, Konstantin