期刊名称：Journal of Nutritional Science and Vitaminology
印刷版ISSN：0301-4800
电子版ISSN：1881-7742
出版年度：1999
卷号：45
期号：4
页码：393-400
DOI：10.3177/jnsv.45.393
出版社：Center for Academic Publications Japan
摘要：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 al-most completely blocked self assembly of the protein. The stoichiometry of ADP-ribose incorporation into unassembled and assembled tubulin was b 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 organi-zation in the brain via the modification of tubulin.
