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Identification of an actin binding region in aldolase
Author(s) -
O'Reilly Gabrielle,
Clarke Frank
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80623-3
Subject(s) - aldolase a , cyanogen bromide , fructose bisphosphate aldolase , actin , aldolase b , biochemistry , actin binding protein , peptide sequence , binding site , actina , homology (biology) , biology , chemistry , cytoskeleton , microbiology and biotechnology , enzyme , actin cytoskeleton , amino acid , gene , cell
Fragmentation of the actin binding glycolytic enzyme, aldolase, with cyanogen bromide yields an 18K actin binding fragment which corresponds to residues 1–164 of the aldolase sequence. Within this fragment there is a region of sequence (residues 32–52) which is highly homologous to a region of sequence near the C‐terminus of actin itself and which is also found in the actin binding domains of a number of other actin binding proteins. A synthetic peptide corresponding to the aldolase sequence 32–52 encompassing this region of homology binds to F‐actin and specifically competes with native aldolase for binding to this cytoskeletal protein.