Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD); National Science Foundation ChinaNational Natural China (NSFC) [71934005, 71903090]; Office the Chief Economist [58-0111-19-013]

Molecular chaperones are thought to inhibit off-pathway interactions such as aggregation from occurring without influencing the on-pathway formation of native structure. Here, we present a mechanism whereby the family of PapD-like chaperones, which are involved in the formation of adhesive pili in pathogenic bacteria, function by suppressing aggregation while simultaneously catalyzing the foldi...

The assembly of adhesive pili from individual subunits by periplasmic PapD-like chaperones in Gram-negative bacteria offers insight into the complex process of organelle biogenesis. PapD-like chaperones bind, stabilize, and cap interactive surfaces of subunits until they are assembled into the pilus. Subunits lack the seventh *gb-strand necessary to complete their immunoglobulin-like folds; the...

A new method for the solid-phase synthesis of enantiomerically enriched highly substituted ring-fused 2-pyridinones 13 has been developed. The synthesis mediates introduction of substituents at two positions in the 2-pyridinone ring in a diverse manner and is suitable for parallel synthesis. (19)F NMR spectroscopy was used as a tool to monitor each of the five steps in the reaction sequence. Th...

The periplasmic PapD-like chaperones have long been known to be necessary for the assembly of bacterial surface organelles. New structural work now suggests that they control assembly by arresting subunit folding. This step may be required to preserve energy for fiber formation.

This work was supported by the National Natural Science Foundation of China under Grant No. 61273070, Doctor Candidate Foundation of Jiangnan University under Grant No. 1252050205135130 and a Project Funded by the Priority Academic Program Development (PAPD) of Jiangsu Higher Education Institutions. *Corresponding author email: [email protected]. Journal of Communications Vol. 9, No. 5, May 2014

“This study was supported by National 973 Program (2012CBA01305); National Science Fund for Outstanding Young Scholars (81322039); National Natural Science Foundation (31371524); Distinguished Young Scholars of Jiangsu Province (BK20130041); Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD); New Century Excellent Talents in University (NCET-13-0870) and the C...

T classic experiments of Anfinsen and his associates established that the primary sequence of a polypeptide contains all of the information needed for a polypeptide to fold into its native fully active tertiary structure (1). Although Anfinsen’s conclusions still hold, for the most part, it is now becoming clear that certain proteins, such as the subunit proteins building up adhesive surface or...

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...