RRC ID 4008
Author Garcia-Dominguez M, March-Diaz R, Reyes JC.
Title The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins.
Journal J Biol Chem
Abstract Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates multiple processes in the eukaryotic cell. In numerous cases sumoylation is facilitated by protein inhibitor of activated STAT (PIAS) proteins, characterized by the presence of a SP-RING domain related to the RING finger of many ubiquitin E3 ligases. The importance of SP-RING relies on its capacity to bind the E2 enzyme of the pathway. Additional domains may participate in SUMO ligase function and target selection. We have studied the Arabidopsis SUMO ligase AtSIZ1, belonging to the PIAS family, and describe self-sumoylation and AtSIZ1-mediated sumoylation of the E2 enzyme AtSCE1 and GTE3, a bromodomain protein interacting with AtSIZ1. Modification of GTE3 modulates its capacity to bind acetyl-histone H3 in vitro. Interestingly, AtSIZ1, as other plant PIAS proteins, also includes a PHD domain. We found that the PHD domain binds AtSCE1 and contributes to the SUMO ligase function, being partially and absolutely required for AtSCE1 and GTE3 sumoylation, respectively. Based on the capacity of AtSCE1 and GTE3 to associate with both the PHD and SP-RING domains, we propose a model of interactions to explain AtSIZ1-mediated sumoylation of GTE3 and ligase function of the PHD domain.
Volume 283(31)
Pages 21469-77
Published 2008-8-1
DOI 10.1074/jbc.M708176200
PII M708176200
PMID 18502747
MeSH Amino Acid Sequence Animals Arabidopsis / enzymology Arabidopsis Proteins / metabolism Gene Expression Regulation, Plant* Genes, Plant Models, Biological Models, Genetic Molecular Sequence Data Mutation Protein Binding Protein Inhibitors of Activated STAT / metabolism* Protein Structure, Tertiary Sequence Homology, Amino Acid Ubiquitin-Protein Ligases / metabolism
IF 4.106
Times Cited 43
Arabidopsis / Cultured plant cells, genes pda10760