Literature DB >> 20957445

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

Rob C A Keller1.   

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.

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Year:  2010        PMID: 20957445      PMCID: PMC6275888          DOI: 10.2478/s11658-010-0036-y

Source DB:  PubMed          Journal:  Cell Mol Biol Lett        ISSN: 1425-8153            Impact factor:   5.787


Supplementary material, approximately 340 KB.
  47 in total

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Journal:  J Bacteriol       Date:  1988-08       Impact factor: 3.490

Review 5.  Protein translocation in Escherichia coli.

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  11 in total

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2.  Identification and in silico analysis of helical lipid binding regions in proteins belonging to the amphitropic protein family.

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4.  Prediction of lipid-binding regions in cytoplasmic and extracellular loops of membrane proteins as exemplified by protein translocation membrane proteins.

Authors:  Rob C A Keller
Journal:  J Membr Biol       Date:  2012-09-09       Impact factor: 1.843

5.  Penetration into membrane of amino-terminal region of SecA when associated with SecYEG in active complexes.

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7.  The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.

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9.  Highly potent antimicrobial peptides from N-terminal membrane-binding region of E. coli MreB.

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10.  Modulation of physiological and pathological activities of lysozyme by biological membranes.

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