Chaperone-assisted self-assembly of pili independent of cellular energy.
作者： F. Jacob-Dubuisson , R. Striker , S.J. Hultgren
DOI: 10.1016/S0021-9258(18)99895-9
关键词:
摘要: Abstract Assembly of P pili on the surface pyelonephritic Escherichia coli proceeds from periplasmic chaperone-subunit complexes. The outer membrane protein PapC, which has been termed a molecular usher, is thought to be site assembly, where chaperone dissociates subunits as they are incorporated into pilus across membrane. kinetics assembly and energy requirements "secretion" events at were investigated using pulse-chase analysis in preformed labeled complexes assembled synchrony by induction PapC. Provided that sufficient amount PapC was present functional membrane, incorporation major PapA subunit shown completed less than 5 min. Our results also indicated targeting may rate-limiting factor for assembly. Following arrival formation seemed proceed spontaneously not sensitive pH shift or an inhibitor electrochemical gradient cytoplasmic We suggest secretion independent cellular thermodynamically driven.
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