ArticleJournal of structural and functional genomics2004
SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins.
Article in Journal of structural and functional genomics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 242 papers.
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Who cites it
242 citing papers in PubMed, 544 citations in OpenAlex.
- Foot-and-mouth disease virus-like particles produced by a SUMO fusion protein system in Escherichia coli induce potent protective immune responses in guinea pigs, swine and cattle.Veterinary research · 2013Trial
- Facile, high-throughput protein purification enabled by high-efficiency protease elution.Protein science : a publication of the Protein Society · 2026Article
- Protocol for efficient purification of endotoxin-free human recombinant tau protein.STAR protocols · 2026Article
- High-yield soluble expression and affinity-tag-free purification of growth hormone receptor antagonist B2036 in Escherichia coli.Bioprocess and biosystems engineering · 2026Article
- ESCRT-III assembles around mis-segregated DNA to protect genome stability.Nature structural & molecular biology · 2026Article
- Protocol for expressing and purifying recombinant full-length Tau by combining affinity chromatography with preparative HPLC.STAR protocols · 2026Article
- The Effect of Protein Tagging on Aggregation and Phase Separation.Journal of cellular biochemistry · 2026Review
- Biochemical characterization of a fungal ice nucleation protein from Podila clonocystis.Scientific reports · 2026Article
- From Sea to Therapy: Development and Analytical Control of Recombinant Human CDKL5 Production in the Marine BacteriumMarine drugs · 2026Article
- Myxarylin: TotalJournal of the American Chemical Society · 2026Article
- Application of a novel fusion tag system for enhanced soluble expression of recombinant proteins in Escherichia coli.BMC biotechnology · 2026Article
- Sensitive detection of cancer antigens enabled by user-defined peptide libraries.Nature biotechnology · 2026Article
- Strategies for enhancing protein solubility: methods, applications, and prospects.NPJ science of food · 2026Review
- Topological reprogramming transforms an integral membrane oligosaccharyltransferase into a water-soluble glycosylation catalyst.bioRxiv : the preprint server for biology · 2026Article
- Human Proteoglycan Linkage Region Glycosyltransferases are Dimeric and Show Unexpected Specificities.Angewandte Chemie (International ed. in English) · 2026Article
- Assessment of Bacterial N-Degron Proteolysis by a Dual-Fluorescence Reporter.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Expression, purification, and crystallization of recombinant human ABL-1 kinase for X-ray crystallography.Turkish journal of chemistry · 2026Article
- A novel chromatography method for high purity production of Recombinant human parathyroid hormone from E. coli.Scientific reports · 2025Article
- A standardized set of pNX vectors for enhanced soluble expression of recombinant proteins in E. coli using small fusion tags.Microbial cell factories · 2025Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
182 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SUMO (small ubiquitin-related modifier) modulates protein structure and function by covalently binding to the lysine side chains of the target proteins. Yeast cells contain two SUMO proteases, Ulp1 and Ulp2, that cleave sumoylated proteins in the cell. Ulp1 (SUMO protease 1) processes the SUMO precursor to its mature form and also de-conjugates SUMO from side chain lysines of target proteins. Here we demonstrate that attachment of SUMO to the N-terminus of under-expressed proteins dramatically enhances their expression in E. coli. SUMO protease 1 was able to cleave a variety of SUMO fusions robustly and with impeccable specificity. Purified recombinant SUMO-GFPs were efficiently cleaved when any amino acid, except proline, was in the+1 position of the cleavage site. The enzyme was active over a broad range of buffer and temperature conditions. Purification of certain recombinant proteins is accomplished by production of Ub-fusions from which Ub can be subsequently removed by de-ubiquitinating enzymes (DUBs). However, DUBs are unstable enzymes that are difficult to produce and inexpensive DUBs are not available commercially. Our findings demonstrate that SUMO protease 1/SUMO-fusion system may be preferable to DUB/Ub-fusion. Enhanced expression and solubility of proteins fused to SUMO combined with broad specificity and highly efficient cleavage properties of the SUMO protease 1 indicates that SUMO-fusion technology will become a useful tool in purification of proteins and peptides.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.