Periplasmic chaperones--preservers of subunit folding energy for organelle assembly.
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.
Behrens
Susanne
S
Department of Molecular Genetics and Preparative Molecular Biology, Institute for Microbiology and Genetics, Georg-August-University Goettingen, Grisebachstrasse 8, D-37077 Goettingen, Germany.
D004734:Energy Metabolism / Q000502:physiology; D029968:Escherichia coli Proteins / Q000378:metabolism*; D005057:Eukaryotic Cells / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D015388:Organelles / Q000378:metabolism*; D019897:Periplasm / Q000378:metabolism*; D033903:Periplasmic Proteins / Q000378:metabolism*; D011387:Prokaryotic Cells / Q000378:metabolism*; D017510:Protein Folding; D020836:Protein Structure, Quaternary / Q000502:physiology; D015010:Yersinia pestis / Q000378:metabolism*
D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C084330:PapD protein, E coli; D033903:Periplasmic Proteins