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

Cellular & Molecular Biology Letters volume 16, pages 40–54 (2011)Cite this article

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.

Abbreviations

DOPC:

1,2-dioleoyl-sn-glycero-3-phosphocholine

DOPG:

1,2-dioleoyl-sn-glycero-3-phosphoglycerol

ESR:

electron spin resonance

HSD:

helical scaffold domain

HWD:

helical wing domain

LBD:

lipid-binding domain

MID:

membrane interacting domain

NBF:

nucleotide-binding fold

PBD:

precursor-binding domain

PE:

phosphatidylethanolamine

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

    Rob C. A. Keller

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Correspondence to Rob C. A. Keller.

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Keller, R.C.A. The prediction of novel multiple lipid-binding regions in protein translocation motor proteins: A possible general feature. Cell Mol Biol Lett 16, 40–54 (2011). https://doi.org/10.2478/s11658-010-0036-y

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Cellular & Molecular Biology Letters

ISSN: 1689-1392

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