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The C‐terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIV f1 function
Author(s) -
Daefler Simon,
Guilvout Ingrid,
Hardie Kim R.,
Pugsley Anthony P.,
Russel Marjorie
Publication year - 1997
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1997.3531727.x
Subject(s) - biology , chaperone (clinical) , bacterial outer membrane , secretion , biophysics , binding site , biochemistry , secretin , bacteriophage , membrane , escherichia coli , microbiology and biotechnology , gene , pathology , medicine
Related outer membrane proteins, termed secretins, participate in the secretion of macromolecules across the outer membrane of many Gram‐negative bacteria. In the pullulanase‐secretion system, PulS, an outer membrane‐associated lipoprotein, is required both for the integrity and the proper outer membrane localization of the PulD secretin. Here we show that the PulS‐binding site is located within the C‐terminal 65 residues of PulD. Addition of this domain to the filamentous phage secretin, pIV, or to the unrelated maltose‐binding protein rendered both proteins dependent on PulS for stability. A chimeric protein composed of bacteriophage f1 pIV and the C‐terminal domain of PulD required properly localized PulS to support phage assembly. An in vivo complex formed between the pIV‐PulD 65 chimera and PulS was detected by co‐immunoprecipitation and by affinity chromatography.