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© The Rockefeller University Press, 0021-9525/1999//981 $5.00
The Journal of Cell Biology, Volume 147, Number 5, , 1999 981-994

Original Article

Cell Cycle–Regulated Attachment of the Ubiquitin-Related Protein Sumo to the Yeast Septins



Erica S. Johnsona and Günter Blobela

a Laboratory of Cell Biology, Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021
Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, 233 South 10th Street, Philadelphia, PA 19107.(215) 503-5393(215) 503-4616

Erica.Johnson{at}mail.tju.edu

SUMO is a ubiquitin-related protein that functions as a posttranslational modification on other proteins. SUMO conjugation is essential for viability in Saccharomyces cerevisiae and is required for entry into mitosis. We have found that SUMO is attached to the septins Cdc3, Cdc11, and Shs1/Sep7 specifically during mitosis, with conjugates appearing shortly before anaphase onset and disappearing abruptly at cytokinesis. Septins are components of a belt of 10-nm filaments encircling the yeast bud neck. Intriguingly, only septins on the mother cell side of the bud neck are sumoylated. We have identified four major SUMO attachment-site lysine residues in Cdc3, one in Cdc11, and two in Shs1, all within the consensus sequence (IVL)KX(ED). Mutating these sites eliminated the vast majority of bud neck-associated SUMO, as well as the bulk of total SUMO conjugates in G2/M-arrested cells, indicating that sumoylated septins are the most abundant SUMO conjugates at this point in the cell cycle. This mutant has a striking defect in disassembly of septin rings, resulting in accumulation of septin rings marking previous division sites. Thus, SUMO conjugation plays a role in regulating septin ring dynamics during the cell cycle.

Key Words: Smt3 • SUMO • septin • cytoskeleton • protein processing

© 1999 The Rockefeller University Press

We are calling the product of the Saccharomyces cerevisiae SMT3 gene SUMO to bring the yeast terminology for this modification in line with the mammalian terminology.

Abbreviations used in this paper: GFP, green fluorescence protein; HA, influenza virus hemagglutinin epitope tag; MALDI-TOF, matrix-assisted laser desorption/ionization time of flight; NTA, nitriloacetic acid; RanGAP1, Ran GTPase-activating protein; ts, temperature sensitive; Ub, ubiquitin.


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