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Fig. 3 | BMC Plant Biology

Fig. 3

From: New perspectives on the plant PARP family: Arabidopsis PARP3 is inactive, and PARP1 exhibits predominant poly (ADP-ribose) polymerase activity in response to DNA damage

Fig. 3

Enzymatic activity of point mutation proteins. a Schematic diagrams of the proteins with point mutations. The residues in the catalytic triad are given in the PARP domain. b The mutated AtPARP1 protein has no catalytic activity. For TRXH-AtPARP1M, the catalytic triad in AtPARP1 was changed from a normal H-Y-E to C-V-E. c Back mutation of the catalytic triad in AtPARP3 cannot recover its activity. For TRXH-AtPARP3M, the catalytic triad in AtPARP3 was changed from C-V-E to a normal H-Y-E. The purified proteins were incubated with 500 nM DNA and 1 mM NAD+ at 25 °C for different time periods with or without 20 mM 3-AB. After the reaction, the proteins were analyzed by immunoblot using different antibodies. The arrows in the Coomassie blue-stained SDS-PAGE gel indicate the recombinant proteins TRXH-AtPARP1 (red arrow), TRXH-AtPARP3 (green arrow), TRXH-AtPARP1M or TRXH-AtPARP3M (black arrow)

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BMC Plant Biology

ISSN: 1471-2229

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