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预测蛋白转位马达蛋白中的新型多脂结合区:一种可能的普遍特征。

The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: a possible general feature.

机构信息

Section Chemistry, Charlemagne College, Wilhelminastraat 13-15, Nijmegen, 3913 NH, The Netherlands.

出版信息

Cell Mol Biol Lett. 2011 Mar;16(1):40-54. doi: 10.2478/s11658-010-0036-y. Epub 2010 Oct 19.

DOI:10.2478/s11658-010-0036-y
PMID:20957445
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6275888/
Abstract

Protein translocation is an important cellular process. SecA is an essential protein component in the Sec system, as it contains the molecular motor that facilitates protein translocation. In this study, a bioinformatics approach was applied in the search for possible lipid-binding helix regions in protein translocation motor proteins. Novel lipid-binding regions in Escherichia coli SecA were identified. Remarkably, multiple lipid-binding sites were also identified in other motor proteins such as BiP, which is involved in ER protein translocation. The prokaryotic signal recognition particle receptor FtsY, though not a motor protein, is in many ways related to SecA, and was therefore included in this study. The results demonstrate a possible general feature for motor proteins involved in protein translocation.

摘要

蛋白质易位是一种重要的细胞过程。SecA 是 Sec 系统中的一种必需蛋白成分,因为它包含促进蛋白质易位的分子马达。在这项研究中,应用了一种生物信息学方法来寻找蛋白质易位马达蛋白中可能的脂质结合螺旋区域。在大肠杆菌 SecA 中发现了新的脂质结合区域。值得注意的是,还在其他马达蛋白中鉴定到了多个脂质结合位点,例如参与 ER 蛋白易位的 BiP。尽管原核信号识别颗粒受体 FtsY 不是一种马达蛋白,但在许多方面与 SecA 相关,因此也包括在本研究中。结果表明,参与蛋白质易位的马达蛋白具有一个可能的普遍特征。

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J Mol Biol. 2009 Jul 17;390(3):401-13. doi: 10.1016/j.jmb.2009.04.061. Epub 2009 May 3.
3
HELIQUEST: a web server to screen sequences with specific alpha-helical properties.HELIQUEST:一个用于筛选具有特定α螺旋特性序列的网络服务器。
Bioinformatics. 2008 Sep 15;24(18):2101-2. doi: 10.1093/bioinformatics/btn392. Epub 2008 Jul 28.
4
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A cleavable N-terminal membrane anchor is involved in membrane binding of the Escherichia coli SRP receptor.一种可裂解的N端膜锚定蛋白参与大肠杆菌信号识别颗粒受体的膜结合。
J Mol Biol. 2008 Mar 28;377(3):761-73. doi: 10.1016/j.jmb.2008.01.040. Epub 2008 Jan 26.
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