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      A new protease required for cell-cycle progression in yeast.

      Nature

      metabolism, Ubiquitins, Substrate Specificity, Small Ubiquitin-Related Modifier Proteins, Sequence Homology, Amino Acid, Saccharomyces cerevisiae Proteins, enzymology, cytology, Saccharomyces cerevisiae, SUMO-1 Protein, Repressor Proteins, genetics, Recombinant Fusion Proteins, Mutagenesis, Molecular Sequence Data, physiology, Mitosis, Humans, G2 Phase, isolation & purification, Fungal Proteins, Escherichia coli, Cysteine Endopeptidases, Cloning, Molecular, Cell Cycle Proteins, Carrier Proteins

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          Abstract

          In eukaryotes, protein function can be modulated by ligation to ubiquitin or to ubiquitin-like proteins (Ubl proteins). The vertebrate Ubl protein SUMO-1 is only 18% identical to ubiquitin but is 48% identical to the yeast protein Smt3. Both SUMO-1 and Smt3 are ligated to cellular proteins, and protein conjugation to SUMO-1/Smt3 is involved in many physiological processes. It remained unknown, however, whether deconjugation of SUMO-1/Smt3 from proteins is also essential. Here we describe a yeast Ubl-specific protease, Ulp1, which cleaves proteins from Smt3 and SUMO-1 but not from ubiquitin. Ulp1 is unrelated to any known deubiquitinating enzyme but shows distant similarity to certain viral proteases, indicating the existence of a widely conserved protease fold. Proteins related to Ulp1 are present in many organisms, including several human pathogens. The pattern of Smt3-coupled proteins in yeast changes markedly throughout the cell cycle, and specific conjugates accumulate in ulp1 mutants. Ulp1 has several functions, including an essential role in the G2/M phase of the cell cycle.

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          Journal
          10.1038/18457
          10094048

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