Outer membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone

Journal of Biological Chemistry

Volumn 286, Issue 45, 2011, Pages 38833-38843

  Nickerson, Nicholas N ^a,b   Tosi, Tommaso ^c,d   Dessen, Andréa ^c,d   Baron, Bruno ^a,b   Raynal, Bertrand ^a,b   England, Patrick ^a,b   Pugsley, Anthony P ^a,b  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

^c INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^d CEA GRENOBLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

C TERMINUS; DISORDERED DOMAINS; DISORDERED REGIONS; HYDRODYNAMIC MEASUREMENTS; IN-VITRO; IN-VIVO; LIMITED PROTEOLYSIS; MULTIMERIZATION; NANOMOLAR AFFINITY; OUTER MEMBRANE; S-DOMAIN; SECONDARY STRUCTURES; TYPE II;

MASS SPECTROMETRY;

DICHROISM;

CHAPERONE; PULD PROTEIN; PULLULANASE; PULS PROTEIN; SECRETIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL OUTER MEMBRANE; BACTERIAL SECRETION SYSTEM; BINDING AFFINITY; BINDING SITE; CHAPERONE BINDING DOMAIN; CIRCULAR DICHROISM; COMPLEX FORMATION; HYDRODYNAMICS; MASS SPECTROMETRY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; STOICHIOMETRY; TYPE II SECRETION SYSTEM;

BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL SECRETION SYSTEMS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; LIPOPROTEINS; MOLECULAR CHAPERONES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

BACTERIA (MICROORGANISMS);

EID: 80655144742     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.279851     Document Type: Article

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