Understanding the catalytic abilities of class IV sirtuin OsSRT1 and its linkage to the DNA repair system under stress conditions

Abstract

The roles of sirtuins in plants are slowly unraveling. Regarding OsSRT1, there are only reports of its H3K9Ac deacetylation. Here we detect the other lysine deacetylation sites in histones, H3 and H4. Further, our studies shed light on its dual enzyme capability with preference for mono ADP ribosylation over deacetylation. OsSRT1 can specifically transfer the single ADP ribose group on its substrates in an enzymatic manner. This mono ADPr effect is not well known in plants, more so for deacetylases. The products of this reaction (NAM and ADP ribose) have a negative effect on this enzyme’s action suggesting a tighter regulation. Resveratrol, a natural plant polyphenol proves to be a good activator of this enzyme at 150 ± 40 µM concentration. Under different abiotic stress conditions, we could link this ADP ribosylase activity to the DNA damage repair (DDR) pathway by activating the enzyme PARP1. There is also evidence of OsSRT1′s interaction with the components of DDR machinery. Changes in the extent of different histone deacetylation by OsSRT1 is also related with these stress conditions. Metal stress in plants also influences these enzyme activities. Structurally there is a long C-terminal domain in OsSRT1 in comparison to other classes of plant sirtuins, which is required for its catalysis.