Role of the amino terminal domain in GroES oligomerization.
Digestions of the GroES oligomer with trypsin, chymotrypsin and Glu-C protease from Staphylococcus aureus V8 (V8) have helped to locate three regions in the GroES sequence that are sensitive to limited proteolysis and have provided information of the GroES domains involved in monomer-monomer and GroEL interaction. The removal of the first 20 or 27 amino acids of the N-terminal region of each GroES monomer by trypsin or chymotrypsin respectively, abolish the oligomerization of the GroES complex and its binding to GroEL. The V8-treatment of GroES promotes the breakage of the peptide bond between Glu18 and Thr19 but not the liberation of the N-terminal fragment from the GroES oligomer, which is capable of forming with GroEL a complex active in protein folding. It is deduced from these results that the N-terminal region of the GroES monomer is involved in monomer-monomer interaction, providing experimental evidence that relates some biochemical properties of GroES with its three-dimensional structure at atomic resolution.
Llorca
O
O
Centro Nacional de Biotechnología, CSIC, Madrid, Spain.
Schneider
K
K
Carrascosa
J L
JL
Méndez
E
E
Valpuesta
J M
JM
D000595:Amino Acid Sequence; D001665:Binding Sites; D018835:Chaperonin 10 / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D018834:Chaperonin 60 / Q000378:metabolism / Q000648:ultrastructure; D019281:Dimerization; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017510:Protein Folding; D017421:Sequence Analysis; D012697:Serine Endopeptidases / Q000378:metabolism; D013884:Thiosulfate Sulfurtransferase / Q000378:metabolism
D018835:Chaperonin 10; D018834:Chaperonin 60; D013884:Thiosulfate Sulfurtransferase; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase