Molecular chaperones: clamps for the Clps?
The Clp/Hsp100 molecular chaperones are unusual in their ability to tease apart protein aggregates and complexes. Recent results make a good case that these chaperones bind substrates via PDZ-like domains; this may reflect a general strategy for manipulating the] assembly state of substrate proteins.
Feng
H P
HP
Department of Chemistry, University of Massachusetts, Amherst 01003, USA.
Gierasch
L M
LM
D000074183:ATPases Associated with Diverse Cellular Activities; D000251:Adenosine Triphosphatases / Q000378:metabolism; D049071:Endopeptidase Clp; D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology; D013379:Substrate Specificity
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D010446:Peptide Fragments; D015800:Protozoan Proteins; D012697:Serine Endopeptidases; D049071:Endopeptidase Clp; D000251:Adenosine Triphosphatases; C095049:ClpB protein, Leishmania; C088072:ClpX protein, E coli; D000074183:ATPases Associated with Diverse Cellular Activities