In‐vitro studies on the folding characteristics of the Escherichia coli precursor protein prePhoE: Evidence that SecB prevents the precursor from aggregating by forming A functional complex

Eefjan Breukink, Ron Kusters, Ben De Kruijff

    Research output: Contribution to journalArticleAcademicpeer-review

    33 Citations (Scopus)
    1 Downloads (Pure)

    Abstract

    We characterised the behaviour of the purified precursor protein prePhoE upon dilution from 8 M urea by CD, fluorescence spectroscopy and gel‐filtration techniques. It is demonstrated that prePhoE rapidly adopts β structure, folds and aggregates upon dilution to urea concentrations below 3 M. These processes are paralleled by a loss of translocation competence. Furthermore the interaction of prePhoE with SecB was investigated. SecB is shown to have a very high content of β structure, therefore we propose that precursor recognition by SecB is mediated through β‐β interaction. It is shown that SecB has little effect on the adoption of secondary structure and tertiary folding upon dilution of the precursor from urea. However, SecB prevents the precursor from aggregating by forming a functional and stable complex.

    Original languageEnglish
    Pages (from-to)419-425
    Number of pages7
    JournalEuropean journal of biochemistry
    Volume208
    Issue number2
    DOIs
    Publication statusPublished - 1 Jan 1992

    Fingerprint Dive into the research topics of 'In‐vitro studies on the folding characteristics of the Escherichia coli precursor protein prePhoE: Evidence that SecB prevents the precursor from aggregating by forming A functional complex'. Together they form a unique fingerprint.

    Cite this