The actin-depolymerizing factor destrin has an actin-stabilizing domain.
Destrin is a 19 kDa actin-depolymerizing protein of the ADF-cofilin family. Destrin was digested with trypsin to a structurally stable 9.2 kDa fragment that contains the actin-binding sequence. The purified 9.2 kDa fragment has an actin filament stabilizing activity, rather than an actin filament depolymerizing activity. The deleted region is probably essential for the actin filament depolymerizing activity of intact destrin. Surprisingly, the 9.2 kDa fragment also has an assembly-promoting activity in the absence of ATP.
Tokuraku
K
K
Department of Chemical Science and Engineering, Miyakonojo National College of Technology, Miyazaki, Japan. tokuraku@miyakonojo-nct.ac.jp
Okamoto
S
S
Katsuki
M
M
Nakagawa
H
H
Kotani
S
S
D051339:Actin Depolymerizing Factors; D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000502:physiology; D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D003598:Cytoskeletal Proteins; D051345:Destrin; D018482:Muscle, Skeletal / Q000201:enzymology; D017434:Protein Structure, Tertiary; D011817:Rabbits
D051339:Actin Depolymerizing Factors; D000199:Actins; D002352:Carrier Proteins; D003598:Cytoskeletal Proteins; D051345:Destrin; D000255:Adenosine Triphosphate