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阪崎肠杆菌ProP C末端卷曲螺旋结构域在耐渗透压方面的作用。

The role of the Cronobacter sakazakii ProP C-terminal coiled coil domain in osmotolerance.

作者信息

Feeney Audrey, Johnston Christopher D, Lucid Alan, O'Mahony Jim, Coffey Aidan, Lucey Brigid, Sleator Roy D

机构信息

Department of Biological Sciences, Cork Institute of Technology, Rossa Avenue, Bishopstown, Cork Ireland.

出版信息

Gut Pathog. 2014 Dec 16;6(1):46. doi: 10.1186/s13099-014-0046-9. eCollection 2014.

DOI:10.1186/s13099-014-0046-9
PMID:25530808
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4272814/
Abstract

BACKGROUND

We investigate the role of the C-terminal coiled coil of the secondary proline porter ProP in contributing to Cronobacter sakazakii osmotolerance.

FINDINGS

The extended C-terminal domain of ProP1 (encoded by ESA_02131) was spliced onto the truncated C-terminal end of ProP2 (encoded by ESA_01706); creating a chimeric protein (ProPc) which exhibits increased osmotolerance relative to the wild type.

CONCLUSIONS

It appears that the C-terminal coiled coil domain tunes ProP at low osmolality, whereas ProP transporters lacking the coiled coil domain are more active at a higher osmolality range.

摘要

背景

我们研究了次级脯氨酸转运蛋白ProP的C末端卷曲螺旋在阪崎肠杆菌耐渗透压方面的作用。

研究结果

将ProP1(由ESA_02131编码)的延伸C末端结构域拼接至ProP2(由ESA_01706编码)的截短C末端;产生了一种嵌合蛋白(ProPc),其相对于野生型表现出更高的耐渗透压性。

结论

似乎C末端卷曲螺旋结构域在低渗透压下调节ProP,而缺乏卷曲螺旋结构域的ProP转运蛋白在较高渗透压范围内更具活性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e37/4272814/66828a537992/13099_2014_46_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e37/4272814/41fcef5a9a32/13099_2014_46_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e37/4272814/66828a537992/13099_2014_46_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e37/4272814/41fcef5a9a32/13099_2014_46_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8e37/4272814/66828a537992/13099_2014_46_Fig2_HTML.jpg

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