Plant SUMO E3 Ligases: Function, Structural Organization, and Connection With DNA

PHD domains and E3 ubiquitin ligases: viruses make the connection.

PHD domains constitute a widely distributed subfamily of zinc fingers whose biochemical functions have been unclear until now. Recently, several PHD-containing viral proteins have been identified that promote immune evasion by downregulating proteins that govern immune recognition. Studies show that these viral regulators lead to ubiquitination of their targets by functioning as E3 ubiquitin li...

MMS21/HPY2 and SIZ1, Two Arabidopsis SUMO E3 Ligases, Have Distinct Functions in Development

The small ubiquitin related modifier (SUMO)-mediated posttranslational protein modification is widely conserved among eukaryotes. Similar to ubiquitination, SUMO modifications are attached to the substrate protein through three reaction steps by the E1, E2 and E3 enzymes. To date, multiple families of SUMO E3 ligases have been reported in yeast and animals, but only two types of E3 ligases have...

PIAS proteins and transcriptional regulation--more than just SUMO E3 ligases?

The PIAS family of proteins was named based on the identification of the founding member, PIAS3, as a repressor of the activity of the STAT3 transcription factor (Protein Inhibitor of Activated STAT) (Chung et al. 1997). Since then, three additional family members— PIAS1, PIASy, and PIASx—have been identified and are characterized by a high degree of sequence conservation throughout the protein...

SUMO E3 Ligases GmSIZ1a and GmSIZ1b regulate vegetative growth in soybean† 

SIZ1 is a small ubiquitin-related modifier (SUMO) E3 ligase that mediates post-translational SUMO modification of target proteins and thereby regulates developmental processes and hormonal and environmental stress responses in Arabidopsis. However, the role of SUMO E3 ligases in crop plants is largely unknown. Here, we identified and characterized two Glycine max (soybean) SUMO E3 ligases, GmSI...

Adenovirus E3 Ubiquitin Ligases