A new protease required for cell-cycle progression in yeast - PubMed (original) (raw)
. 1999 Mar 18;398(6724):246-51.
doi: 10.1038/18457.
Affiliations
- PMID: 10094048
- DOI: 10.1038/18457
A new protease required for cell-cycle progression in yeast
S J Li et al. Nature. 1999.
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.
Similar articles
- The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein.
Li SJ, Hochstrasser M. Li SJ, et al. Mol Cell Biol. 2000 Apr;20(7):2367-77. doi: 10.1128/MCB.20.7.2367-2377.2000. Mol Cell Biol. 2000. PMID: 10713161 Free PMC article. - Smt3, a SUMO-1 homolog, is conjugated to Cdc3, a component of septin rings at the mother-bud neck in budding yeast.
Takahashi Y, Iwase M, Konishi M, Tanaka M, Toh-e A, Kikuchi Y. Takahashi Y, et al. Biochem Biophys Res Commun. 1999 Jun 16;259(3):582-7. doi: 10.1006/bbrc.1999.0821. Biochem Biophys Res Commun. 1999. PMID: 10364461 - A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex.
Reverter D, Lima CD. Reverter D, et al. Structure. 2004 Aug;12(8):1519-31. doi: 10.1016/j.str.2004.05.023. Structure. 2004. PMID: 15296745 - SUMO-specific proteases: a twist in the tail.
Hay RT. Hay RT. Trends Cell Biol. 2007 Aug;17(8):370-6. doi: 10.1016/j.tcb.2007.08.002. Epub 2007 Sep 4. Trends Cell Biol. 2007. PMID: 17768054 Review. - Modification in reverse: the SUMO proteases.
Mukhopadhyay D, Dasso M. Mukhopadhyay D, et al. Trends Biochem Sci. 2007 Jun;32(6):286-95. doi: 10.1016/j.tibs.2007.05.002. Epub 2007 May 17. Trends Biochem Sci. 2007. PMID: 17499995 Review.
Cited by
- Interplay between viruses and host sumoylation pathways.
Everett RD, Boutell C, Hale BG. Everett RD, et al. Nat Rev Microbiol. 2013 Jun;11(6):400-11. doi: 10.1038/nrmicro3015. Epub 2013 Apr 29. Nat Rev Microbiol. 2013. PMID: 23624814 Review. - Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. atomic resolution structure of the nascent form of the adenovirus proteinase.
Baniecki ML, McGrath WJ, Mangel WF. Baniecki ML, et al. J Biol Chem. 2013 Jan 18;288(3):2081-91. doi: 10.1074/jbc.M112.407429. Epub 2012 Oct 7. J Biol Chem. 2013. PMID: 23043139 Free PMC article. - SUMOylation in control of accurate chromosome segregation during mitosis.
Wan J, Subramonian D, Zhang XD. Wan J, et al. Curr Protein Pept Sci. 2012 Aug;13(5):467-81. doi: 10.2174/138920312802430563. Curr Protein Pept Sci. 2012. PMID: 22812528 Free PMC article. Review. - Discovery of small molecule inhibitors of ubiquitin-like poxvirus proteinase I7L using homology modeling and covalent docking approaches.
Katritch V, Byrd CM, Tseitin V, Dai D, Raush E, Totrov M, Abagyan R, Jordan R, Hruby DE. Katritch V, et al. J Comput Aided Mol Des. 2007 Oct-Nov;21(10-11):549-58. doi: 10.1007/s10822-007-9138-7. Epub 2007 Oct 25. J Comput Aided Mol Des. 2007. PMID: 17960327 Free PMC article. - In Vitro Assembly of Diverse Bacterial Microcompartment Shell Architectures.
Hagen AR, Plegaria JS, Sloan N, Ferlez B, Aussignargues C, Burton R, Kerfeld CA. Hagen AR, et al. Nano Lett. 2018 Nov 14;18(11):7030-7037. doi: 10.1021/acs.nanolett.8b02991. Epub 2018 Oct 31. Nano Lett. 2018. PMID: 30346795 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases