PMID:9684869: Difference between revisions

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<span style = 'font-size: large'> '''van Klompenburg, W, Paetzel, M, de Jong, JM, Dalbey, RE, Demel, RA, von Heijne, G and de Kruijff, B'''  (1998) Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes.''FEBS Lett.'' '''431''':75-9</span>
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'''van Klompenburg, W, Paetzel, M, de Jong, JM, Dalbey, RE, Demel, RA, von Heijne, G and de Kruijff, B'''  (1998) Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes. ''FEBS Lett.'' '''431''':75-9
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!align=left  |Abstract
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Leader peptidase is an integral membrane protein of E. coli and it catalyses the removal of most signal peptides from translocated precursor proteins. In this study it is shown that when the transmembrane anchors are removed in vivo, the remaining catalytic domain can bind to inner and outer membranes of E. coli. Furthermore, the purified catalytic domain binds to inner membrane vesicles and vesicles composed of purified inner membrane lipids with comparable efficiency. It is shown that the interaction is caused by penetration of a part of the catalytic domain between the lipids. Penetration is mediated by phosphatidylethanolamine, the most abundant lipid in E. coli, and does not seem to depend on electrostatic interactions. A hydrophobic segment around the catalytically important residue serine 90 is required for the interaction with membranes.
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[http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9684869 PubMed]


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|{{TableHeadingColor}} |'''Abstract''' || Leader peptidase is an integral membrane protein of E. coli and it catalyses the removal of most signal peptides from translocated precursor proteins. In this study it is shown that when the transmembrane anchors are removed in vivo, the remaining catalytic domain can bind to inner and outer membranes of E. coli. Furthermore, the purified catalytic domain binds to inner membrane vesicles and vesicles composed of purified inner membrane lipids with comparable efficiency. It is shown that the interaction is caused by penetration of a part of the catalytic domain between the lipids. Penetration is mediated by phosphatidylethanolamine, the most abundant lipid in E. coli, and does not seem to depend on electrostatic interactions. A hydrophobic segment around the catalytically important residue serine 90 is required for the interaction with membranes.
!align=left  |Keywords
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Amino Acid Sequence; Binding Sites; Biological Transport; Catalysis; Cell Membrane/metabolism; Escherichia coli/metabolism; Lipid Bilayers/metabolism; Membrane Lipids/metabolism; Membrane Proteins/metabolism; Molecular Sequence Data; Phosphatidylethanolamines/metabolism; Protein Binding; Serine Endopeptidases/metabolism
|{{TableHeadingColor}} nowrap |'''Links''' ||  [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=9684869 PubMed]
 
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==Annotations {{HelpIcon|Help:Literature}}==
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Latest revision as of 05:05, 15 September 2013

Citation

van Klompenburg, W, Paetzel, M, de Jong, JM, Dalbey, RE, Demel, RA, von Heijne, G and de Kruijff, B (1998) Phosphatidylethanolamine mediates insertion of the catalytic domain of leader peptidase in membranes. FEBS Lett. 431:75-9

Abstract

Leader peptidase is an integral membrane protein of E. coli and it catalyses the removal of most signal peptides from translocated precursor proteins. In this study it is shown that when the transmembrane anchors are removed in vivo, the remaining catalytic domain can bind to inner and outer membranes of E. coli. Furthermore, the purified catalytic domain binds to inner membrane vesicles and vesicles composed of purified inner membrane lipids with comparable efficiency. It is shown that the interaction is caused by penetration of a part of the catalytic domain between the lipids. Penetration is mediated by phosphatidylethanolamine, the most abundant lipid in E. coli, and does not seem to depend on electrostatic interactions. A hydrophobic segment around the catalytically important residue serine 90 is required for the interaction with membranes.

Links

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Keywords

Amino Acid Sequence; Binding Sites; Biological Transport; Catalysis; Cell Membrane/metabolism; Escherichia coli/metabolism; Lipid Bilayers/metabolism; Membrane Lipids/metabolism; Membrane Proteins/metabolism; Molecular Sequence Data; Phosphatidylethanolamines/metabolism; Protein Binding; Serine Endopeptidases/metabolism

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