Mouse RT6 locus 1 and rat RT6.2 are NAD+. Arginine ADP-ribosyltransferases with auto-ADP-ribosylation activity

Authors
Bortell, Rita
Rigby, Mark R.
Stevens, Linda A.
Moss, Joel
Kanaitsuka, Toshihiro
Mordes, John P.
Greiner, Dale L.
Rossini, Aldo A.
UMass Chan Affiliations
Department of Medicine, Division of Endocrinology and Metabolism
Department of Medicine, Diabetes Division
Graduate School of Biomedical Sciences
Document Type
Article
Publication Date
1997-01-01
Keywords
ADP Ribose Transferases; Adenosine Diphosphate Ribose; Animals; Antigens, Differentiation, T-Lymphocyte; Catalysis; Cell Division; Cell Line; Histocompatibility Antigens; Linkage (Genetics); *Membrane Glycoproteins; Mice; NAD; Precipitin Tests; Rats; Recombinant Fusion Proteins; Spodoptera; T-Lymphocytes
Life Sciences
Medicine and Health Sciences

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Link to Full Text
http://www.jimmunol.org/content/156/11/4259
Abstract
We report that rat RT6.2 and recombinant mouse Rt6 locus 1 proteins possess auto-ADP-ribosyltransferase activity and that Rt6, but not RT6, catalyzes the ADP-ribosylation of exogenous histones. Based on NH2OH sensitivity, it appeared that the ADP-ribose was attached to arginine residues on proteins. We also observed that the NAD+ concentration in culture medium correlates inversely with the proliferation of rat RT6+ T cells. The data suggest that lymphocyte surface ADP-ribosyltransferases could be involved in signaling and immunoregulatory processes.
Source
Adv Exp Med Biol. 1997;419:169-73.
Permanent Link to this Item
http://hdl.handle.net/20.500.14038/32566
PubMed ID
9193650
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