Covalent attachment of the ubiquitin-related protein SUMO to other proteins
participates in many processes including signal transduction, transcriptio
nal regulation, and growth control. We report the characterization of Siz1
as an E3-like factor in the SUMO pathway. Siz1 is required for SUMO attachm
ent to the S. cerevisiae septins in vivo and strongly stimulates septin sum
oylation in vitro. Siz1 and the related protein Siz2 promote SUMO conjugati
on to different substrates at different stages of the cell cycle and, toget
her, are required for most SUMO conjugation in yeast. Siz1, Siz2, and the P
IAS (protein inhibitor of activated STAT) proteins form a conserved family
defined by an unusual RING-related motif. Our results suggest that this fam
ily functions by promoting SUMO conjugation to specific substrates.