NDLI: Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper

Content Provider	PubMed Central
Author	Bullitt, Esther Jones, C. hal Striker, Robert Soto, Gabriel Jacob-dubuisson, Françoise Pinkner, Jerome Wick, Mary jo Makowski, Lee Hultgren, Scott j.
Copyright Year	1996
Abstract	The major subassemblies of virulence-associated P pili, the pilus rod (comprised of PapA) and tip fibrillum (comprised of PapE), were reconstituted from purified chaperone-subunit complexes in vitro. Subunits are held in assembly-competent conformations in chaperone-subunit complexes prior to their assembly into mature pili. The PapD chaperone binds, in part, to a conserved motif present at the C terminus of the subunits via a beta zippering interaction. Amino acid residues in this conserved motif were also found to be essential for subunit–subunit interactions necessary for the formation of pili, thus revealing a molecular mechanism whereby the PapD chaperone may prevent premature subunit–subunit interactions in the periplasm. Uncapping of the chaperone-protected C terminus of PapA and PapE was mimicked in vitro by freeze–thaw techniques and resulted in the formation of pilus rods and tip fibrillae, respectively. A mutation in the leading edge of the beta zipper of PapA produces pilus rods with an altered helical symmetry and azimuthal disorder. This change in the number of subunits per turn of the helix most likely reflects involvement of the leading edge of the beta zipper in forming a right-handed helical cylinder. Organelle development is a fundamental process in all living cells, and these studies shed new light on how immunoglobulin-like chaperones govern the formation of virulence-associated organelles in pathogenic bacteria.
Starting Page	12890
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	93
Language	English
Publisher	The National Academy of Sciences of the USA
Publisher Date	1996-11-12
Access Restriction	Open
Rights Holder	The National Academy of Sciences of the USA
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper.

PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.

Structural basis of chaperone self-capping in P pilus biogenesis

Outer-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.

Immunoglobulin-like PapD chaperone caps and uncaps interactive surfaces of nascently translocated pilus subunits.

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PapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbA.

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Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper

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Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper.

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Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper