title: ADP-ribosylation of Arg28 and Arg206 on the actin molecule by chicken arginine-specific ADP-ribosyltransferase.
abstract: We reported previously on ADP-ribosylation of actins by chicken arginine-specific ADP-ribosyltransferase in vitro and in situ and the inhibition of actin polymerization by this modification [Terashima, M., Mishima, K., Yamada, K., Tsuchiya, M., Wakutani, T. & Shimoyama, M. (1992) Eur. J. Biochem. 204, 305-311]. In the present study, we determined amino acid residues of ADP-ribosylation site(s) in globular (G-) and filamentous (F-) actins and examined the molecular basis of the modification of actin. Arginine-specific ADP-ribosylation occurred at Arg28 and Arg206 in G-actin, but only at Arg28 in F-actin. ADP-ribosylation of Arg206, located on the pointed end of the actin molecule, significantly blocked the interaction with deoxyribonuclease I. These results indicate that Arg206 in G-actin may be involved in actin polymerization. ADP-ribosylation of Arg28, located on the outer surface of actin molecule, did not affect the binding activity with myosin subfragment-1, that is thought to interact through the N-terminal amino acid residues of G-actin. ADP-ribosylation at both Arg28 and Arg206 of G-actin had no apparent effect on the intrinsic ATPase activity. We concluded from this study that ADP-ribosylation of Arg206 in G-actin causes the inhibition of actin polymerization, and that ADP-ribosylation of Arg28 occurs in F-actin.
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: Shimoyama
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001120:Arginine / Q000378:metabolism*; D002645:Chickens; D003850:Deoxyribonuclease I / Q000378:metabolism; D008969:Molecular Sequence Data; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D000199:Actins; D000246:Adenosine Diphosphate Ribose; D001120:Arginine; D011065:Poly(ADP-ribose) Polymerases; D003850:Deoxyribonuclease I; D000251:Adenosine Triphosphatases