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Volume 271, Number 47, Issue of November 22, 1996 pp. 29552-29555
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Glutamic Acid 207 in Rodent T-cell RT6 Antigens Is Essential for Arginine-specific ADP-ribosylation

(Received for publication, April 5, 1996, and in revised form, August 27, 1996)

From the Department of Biochemistry, Shimane Medical University, 89-1, Izumo, Shimane 693, Japan

A rat T-cell antigen RT6.1 catalyzes NAD glycohydrolysis but not ADP-ribose transfer, even though the antigen has significant amino acid identity with eucaryotic arginine-specific ADP-ribosyltransferases. Since a highly conserved Glu in the catalytic region of these transferases is substituted with Gln at position 207 in RT6.1, we replaced the Gln with Glu, Asp, or Ala, by site-directed mutagenesis. The Glu-207 mutant produced ADP-ribosylarginine during incubation with NAD and L-arginine. The Asp-207 mutant but not the Ala-207 mutant produced ADP-ribosylarginine, but at a lower rate. In contrast, these mutations affected NAD glycohydrolase activity of RT6.1 to a much lesser extent. Kinetic studies of transferase reaction revealed that k_cat of the Glu-207 mutant increased compared to findings with the Asp-207 mutant. Moreover, the mouse homologue of rat RT6 lost arginine-specific ADP-ribosyltransferase activity when Glu-207 was replaced with Gln. Thus, Glu-207 in rodent T-cell RT6 antigens is essential for transfer reaction of ADP-ribose to arginine.

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