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A new protease required for cell-cycle progression in yeast

Author

Listed:
  • Shyr-Jiann Li

    (University of Chicago)

  • Mark Hochstrasser

    (University of Chicago)

Abstract

In eukaryotes, protein function can be modulated by ligation to ubiquitin or to ubiquitin-like proteins (Ubl proteins)1,2,3. 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 processes3,4,5,6,7,8,9,10. 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.

Suggested Citation

  • Shyr-Jiann Li & Mark Hochstrasser, 1999. "A new protease required for cell-cycle progression in yeast," Nature, Nature, vol. 398(6724), pages 246-251, March.
    • Handle: RePEc:nat:nature:v:398:y:1999:i:6724:d:10.1038_18457
    DOI: 10.1038/18457
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    Cited by:

    1. Xue-Ming Wu & Bo-Sen Zhang & Yun-Long Zhao & Hua-Wei Wu & Feng Gao & Jie Zhang & Jian-Hua Zhao & Hui-Shan Guo, 2023. "DeSUMOylation of a Verticillium dahliae enolase facilitates virulence by derepressing the expression of the effector VdSCP8," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    2. Joana S. Rodrigues & Miguel Chenlo & Susana B. Bravo & Sihara Perez-Romero & Maria Suarez-Fariña & Tomas Sobrino & Rebeca Sanz-Pamplona & Román González-Prieto & Manuel Narciso Blanco Freire & Ruben N, 2024. "dsRNAi-mediated silencing of PIAS2beta specifically kills anaplastic carcinomas by mitotic catastrophe," Nature Communications, Nature, vol. 15(1), pages 1-30, December.
    3. Ying Li & Nathalia Varejão & David Reverter, 2022. "Structural basis for the SUMO protease activity of the atypical ubiquitin-specific protease USPL1," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    4. Matthijs P. Hoelscher & Joachim Forner & Silvia Calderone & Carolin Krämer & Zachary Taylor & F. Vanessa Loiacono & Shreya Agrawal & Daniel Karcher & Fabio Moratti & Xenia Kroop & Ralph Bock, 2022. "Expression strategies for the efficient synthesis of antimicrobial peptides in plastids," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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