Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.

Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction ...
of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.
Mesh Terms:
Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, Cysteine Endopeptidases, Fungal Proteins, Glycine, Models, Molecular, Molecular Sequence Data, Peptide Fragments, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Small Ubiquitin-Related Modifier Proteins, Substrate Specificity, Surface Properties, Ubiquitins
Mol. Cell
Date: May. 01, 2000
Download Curated Data For This Publication
16333
Switch View:
  • Interactions 1