TY - JOUR
T1 - PapD-like chaperones provide the missing information for folding of pilin proteins
AU - Barnhart, Michelle M.
AU - Pinkner, Jerome S.
AU - Soto, Gabriel E.
AU - Sauer, Frederic G.
AU - Langermann, Sol
AU - Waksman, Gabriel
AU - Frieden, Carl
AU - Hultgren, Scott J.
PY - 2000/7/5
Y1 - 2000/7/5
N2 - A fundamental question in molecular biology is how proteins fold into domains that can serve as assembly modules for building up large macromolecular structures. The biogenesis of pili on the surface of Gram- negative bacteria requires the orchestration of a complex process that includes protein synthesis, folding via small chaperones, secretion, and assembly. The results presented here support the hypothesis that pilus subunit folding and biogenesis proceed via mechanisms termed donor strand complementation and donor strand exchange. Here we show that the steric information necessary for pilus subunit folding is not contained in one polypeptide sequence. Rather, the missing information is transiently donated by a strand of a small chaperone to allow folding. Providing the missing information for folding, via a 13-amino acid peptide extension to the C- terminal end of a pilus subunit, resulted in the production of a protein that no longer required the chaperone to fold. This mechanism of small periplasmic chaperone function described here deviates from classical hsp60 chaperone- assisted folding.
AB - A fundamental question in molecular biology is how proteins fold into domains that can serve as assembly modules for building up large macromolecular structures. The biogenesis of pili on the surface of Gram- negative bacteria requires the orchestration of a complex process that includes protein synthesis, folding via small chaperones, secretion, and assembly. The results presented here support the hypothesis that pilus subunit folding and biogenesis proceed via mechanisms termed donor strand complementation and donor strand exchange. Here we show that the steric information necessary for pilus subunit folding is not contained in one polypeptide sequence. Rather, the missing information is transiently donated by a strand of a small chaperone to allow folding. Providing the missing information for folding, via a 13-amino acid peptide extension to the C- terminal end of a pilus subunit, resulted in the production of a protein that no longer required the chaperone to fold. This mechanism of small periplasmic chaperone function described here deviates from classical hsp60 chaperone- assisted folding.
UR - http://www.scopus.com/inward/record.url?scp=0034608863&partnerID=8YFLogxK
U2 - 10.1073/pnas.130183897
DO - 10.1073/pnas.130183897
M3 - Article
C2 - 10859353
AN - SCOPUS:0034608863
SN - 0027-8424
VL - 97
SP - 7709
EP - 7714
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 14
ER -