Evidence for the participation of histidine residues located in the 56 kDa C-terminal polypeptide domain of ADP-ribosyl transferase in its catalytic activity

Purified ADPRT protein was inactivated by the histidine specific reagent diethylpyrocarbonate, binding to two histidine residues, or by a relatively histidine selective photoinactivation method. Inactivation with up to 1.3 mM diethylpyrocarbonate was reversible by hydroxylamine. Enzymatic inactivati...

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Bibliographic Details
Published in:FEBS letters 1990-10, Vol.273 (1-2), p.6-10
Main Authors: Bauer, Pal I., Buki, Kaiman G., Kun, Ernest
Format: Article
Language:English
Subjects:
ADP-ribosylation
ADP-ribosyltransferase
Analytical, structural and metabolic biochemistry
Binding Sites
Biological and medical sciences
Catalytic domain of ADPRT
Cellulose - analogs & derivatives
Diethyl Pyrocarbonate - pharmacology
Diethylpyrocarbonate
DNA
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Histidine
Histidine residue
Hydroxylamine
Hydroxylamines - pharmacology
Kinetics
Light
Photoactivation
Poly(ADP-ribose) Polymerase Inhibitors
Poly(ADP-ribose) Polymerases - metabolism
Poly(ADP-ribose) Polymerases - radiation effects
Protein Binding
Rose Bengal - pharmacology
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Summary:Purified ADPRT protein was inactivated by the histidine specific reagent diethylpyrocarbonate, binding to two histidine residues, or by a relatively histidine selective photoinactivation method. Inactivation with up to 1.3 mM diethylpyrocarbonate was reversible by hydroxylamine. Enzymatic inactivation coincided with the loss of binding capacity of the enzyme protein to benzamide affinity matrix but not to DNA cellulose. Labelled diethylpyrocarbonate was identified exclusively in the 56 kDa carboxyl-terminal polypeptide where 2 out of 13 histidine residues were modified by this reagent. It is proposed that histidine residues in the 56 kDa polypeptide may participate as initiator sites for polyADP-ribosylation.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(90)81038-P