A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
- PMID: 15296745
- DOI: 10.1016/j.str.2004.05.023
A basis for SUMO protease specificity provided by analysis of human Senp2 and a Senp2-SUMO complex
Abstract
Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear metabolism and cell cycle progression in yeast. X-ray structures of the human Senp2 catalytic protease domain and of a covalent thiohemiacetal transition-state complex obtained between the Senp2 catalytic domain and SUMO-1 revealed details of the respective protease and substrate surfaces utilized in interactions between these two proteins. Comparative biochemical and structural analysis between Senp2 and the yeast SUMO protease Ulp1 revealed differential abilities to process SUMO-1, SUMO-2, and SUMO-3 in maturation and deconjugation reactions. Further biochemical characterization of the three SUMO isoforms into which an additional Gly-Gly di-peptide was inserted, or whereby the respective SUMO tails from the three isoforms were swapped, suggests a strict dependence for SUMO isopeptidase activity on residues C-terminal to the conserved Gly-Gly motif and preferred cleavage site for SUMO proteases.
Similar articles
-
Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates.Nat Struct Mol Biol. 2006 Dec;13(12):1060-8. doi: 10.1038/nsmb1168. Epub 2006 Nov 12. Nat Struct Mol Biol. 2006. PMID: 17099700
-
A new protease required for cell-cycle progression in yeast.Nature. 1999 Mar 18;398(6724):246-51. doi: 10.1038/18457. Nature. 1999. PMID: 10094048
-
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.Mol Cell. 2000 May;5(5):865-76. doi: 10.1016/s1097-2765(00)80326-3. Mol Cell. 2000. PMID: 10882122
-
SUMO-specific proteases: a twist in the tail.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.
-
DeSUMOylating enzymes--SENPs.IUBMB Life. 2008 Nov;60(11):734-42. doi: 10.1002/iub.113. IUBMB Life. 2008. PMID: 18666185 Review.
Cited by
-
The SUMO Family: Mechanisms and Implications in Thyroid Cancer Pathogenesis and Therapy.Biomedicines. 2024 Oct 21;12(10):2408. doi: 10.3390/biomedicines12102408. Biomedicines. 2024. PMID: 39457720 Free PMC article. Review.
-
Influenza virus infection causes global RNAPII termination defects.Nat Struct Mol Biol. 2018 Sep;25(9):885-893. doi: 10.1038/s41594-018-0124-7. Epub 2018 Sep 3. Nat Struct Mol Biol. 2018. PMID: 30177761 Free PMC article.
-
Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation.Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11769-74. doi: 10.1073/pnas.1001760107. Epub 2010 Jun 14. Proc Natl Acad Sci U S A. 2010. PMID: 20547879 Free PMC article.
-
Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1.Biochem J. 2005 Mar 1;386(Pt 2):325-30. doi: 10.1042/BJ20041210. Biochem J. 2005. PMID: 15487983 Free PMC article.
-
The Structural Basis of African Swine Fever Virus pS273R Protease Binding to E64 through Molecular Dynamics Simulations.Molecules. 2023 Feb 2;28(3):1435. doi: 10.3390/molecules28031435. Molecules. 2023. PMID: 36771101 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
