title: ADP-ribosylation of tubulin by chicken NAD-arginine ADP-ribosyltransferase suppresses microtubule formation.
abstract: We obtained evidence that tubulin and actin, two major cytoskeletal proteins, are preferentially ADP-ribosylated in the bovine brain cytosol by NAD-arginine ADP-ribosyltransferase purified from chicken polymorphonuclear leukocytes. ADP-ribosylation of tubulin almost completely blocked self-assembly of the protein. The stoichiometry of ADP-ribose incorporation into unassembled and assembled tubulin was 6 and 2 mol/mol of tubulin, respectively. These findings suggest that sites of ADP-ribosylation in the unassembled tubulin molecule are crucial for tubulin assembly, and that covalently attached ADP-ribose moieties interfere with tubulin interaction by steric hindrance or conformational change. Thus, ADP-ribosylation may be involved in cytoskeletal organization in the brain via the modification of tubulin.
authors.affiliation: Department of Biochemistry, Shimane Medical University, Izumo, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Terashima
authors.forename: C
authors.initials: C
authors.lastname: Yamamori
authors.forename: M
authors.initials: M
authors.lastname: Tsuchiya
authors.forename: M
authors.initials: M
authors.lastname: Shimoyama
mesh_terms: D036002:ADP Ribose Transferases / Q000378:metabolism*; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000378:metabolism / Q000648:ultrastructure; D002417:Cattle; D002645:Chickens; D003600:Cytosol / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008870:Microtubules / Q000502:physiology* / Q000648:ultrastructure; D009243:NAD / Q000494:pharmacology; D009504:Neutrophils / Q000201:enzymology; D014404:Tubulin / Q000378:metabolism*
chemical_list: D014404:Tubulin; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D036002:ADP Ribose Transferases