PMID:3298248
| Citation |
Julin, DA and Lehman, IR (1987) Photoaffinity labeling of the recBCD enzyme of Escherichia coli with 8-azidoadenosine 5'-triphosphate. J. Biol. Chem. 262:9044-51 |
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| Abstract |
The recB and recD subunits of the recBCD enzyme (exonuclease V) from Escherichia coli were covalently photolabeled with the ATP photoaffinity analogue [alpha-32P]8-azido-ATP. The labeling was specific for ATP binding sites by the following criteria. Saturation occurs at high 8-azido-ATP concentrations with dissociation constants of 30 and 120 microM for the recD and recB subunits, respectively; ATP strongly inhibits the photolabeling; 8-azido-ATP is hydrolyzed by the recBCD enzyme and supports its double-stranded DNA exonuclease activity; and the label is largely confined to two peptides obtained by tryptic digestion of the photolabeled holoenzyme; one is derived from the recB subunit and the other from the recD subunit. |
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| Keywords |
Adenosine Triphosphate/analogs & derivatives; Adenosine Triphosphate/metabolism; Affinity Labels/metabolism; Azides/metabolism; Chromatography, High Pressure Liquid; DNA, Viral/metabolism; Escherichia coli/enzymology; Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases/metabolism; Fructose-Bisphosphate Aldolase/metabolism; Macromolecular Substances; Nucleotides/pharmacology; Photochemistry; Plasmids; Trypsin/metabolism |
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