The amino-terminal fragment of gelsolin is cross-linked to Cys-374 of actin in the EGTA-resistant actin-gelsolin complex.
It has been shown that the EGTA-resistant actin, one of the two actin molecules associated to gelsolin, can be predominantly cross-linked to gelsolin by benzophenone-4-maleimide (BPM), a photoaffinity-labeling reagent, which was conjugated to Cys-374 of actin prior to cross-linking (Doi, Y., Banba, M. and Vertut-Doï, A. (1991) Biochemistry 30, 5769-5777). When a chymotryptic digest of gelsolin containing the amino-terminal 15-kDa fragment was mixed with BPM-actin (42 kDa) and irradiated for cross-linking, a band of 58 kDa appeared on SDS-PAGE which was shown to contain actin molecule by using fluorescently labeled actin. The amino-terminal sequence of the 58-kDa complex was identical to that of gelsolin, confirming that the amino-terminal segment (residues 1-133) of pig plasma gelsolin lies closely to Cys-374 of actin in the EGTA-resistant complex.
Doi
Y
Y
Department of Food Science, Kyoto Women's University, Japan.
Kanatani
Y
Y
Kim
F
F
D000199:Actins / Q000737:chemistry*; D000595:Amino Acid Sequence; D000818:Animals; D001577:Benzophenones; D002135:Calcium-Binding Proteins / Q000737:chemistry* / Q000187:drug effects; D002918:Chymotrypsin / Q000494:pharmacology; D003432:Cross-Linking Reagents; D018260:Gelsolin; D046911:Macromolecular Substances; D008301:Maleimides; D008840:Microfilament Proteins / Q000737:chemistry* / Q000187:drug effects; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013552:Swine
D000199:Actins; D001577:Benzophenones; D002135:Calcium-Binding Proteins; D003432:Cross-Linking Reagents; D018260:Gelsolin; D046911:Macromolecular Substances; D008301:Maleimides; D008840:Microfilament Proteins; D010446:Peptide Fragments; C046109:benzophenone-4-maleimide; D002918:Chymotrypsin