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Article

Kinetics and energetics of the translocation of maltose binding protein folding mutants.

Journal of molecular biology - 14 Mar 2008

Tomkiewicz Danuta, Nouwen Nico, Driessen Arnold J M

Abstract excerpt

Protein translocation in Escherichia coli is mediated by the translocase that, in its minimal form, comprises a protein-conducting pore (SecYEG) and a motor protein (SecA). The SecYEG complex forms a narrow channel in the membrane that allows passage of secretory proteins (preproteins) in an unfolded state only. It has been suggested that the SecA requirement for translocation depends on the folding stability of...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 18241889
DOI: 10.1016/j.jmb.2008.01.014

Genes

MBP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Kinetics and energetics of the translocation of maltose binding protein folding mutants.PMID 18241889Read ↗

Interaction of SecB with intermediates along the folding pathway of maltose-binding protein.Semantic proximity Read ↗

Translocation of proteins through the Sec61 and SecYEG channels.Semantic proximity Read ↗

Roles of SecG in ATP- and SecA-dependent protein translocation.Semantic proximity Read ↗

Export of the periplasmic maltose-binding protein of Escherichia coli.Semantic proximity Read ↗

Protein translocation functions of Escherichia coli SecY: in vitro characterization of cold-sensitive secY mutants.Semantic proximity Read ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

Escherichia coli sec mutants accumulate a processed immature form of maltose-binding protein (MBP), a late-phase intermediate in MBP export.Semantic proximity Read ↗

Folding and aggregation of export-defective mutants of the maltose-binding protein.Semantic proximity Read ↗

Mutations of the molecular chaperone protein SecB which alter the interaction between SecB and maltose-binding protein.Semantic proximity Read ↗

Identification of the preprotein binding domain of SecA.Semantic proximity Read ↗

Biochemical characterization of a mutationally altered protein translocase: proton motive force stimulation of the initiation phase of translocation.Semantic proximity Read ↗

The PrlA and PrlG phenotypes are caused by a loosened association among the translocase SecYEG subunits.Semantic proximity Read ↗

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