Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage
| Autor: | D.H. Jones, W. Min, A.J. Dunn |
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| Rok vydání: | 1992 |
| Předmět: |
Models
Molecular Glycosylation animal structures Protein Conformation Molecular Sequence Data macromolecular substances Protein Sorting Signals Chromatography Affinity General Biochemistry Genetics and Molecular Biology law.invention chemistry.chemical_compound Protein structure law Complementary DNA Concanavalin A Escherichia coli Cloning Molecular Protein Precursors Molecular Biology Protein maturation chemistry.chemical_classification Plants Medicinal Base Sequence General Immunology and Microbiology biology General Neuroscience Lectin Fabaceae Recombinant Proteins Molecular Weight carbohydrates (lipids) chemistry Biochemistry biology.protein Recombinant DNA Electrophoresis Polyacrylamide Gel lipids (amino acids peptides and proteins) Plant Lectins Glycoprotein Protein Processing Post-Translational Research Article |
| Zdroj: | The EMBO Journal. 11:1303-1307 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1992.tb05174.x |
| Popis: | The complex post-translational processing of concanavalin A (Con A) in maturing jackbeans is unique because the non-glycosylated mature active protein is circularly permuted in primary sequence relative to its own inactive precursor (glycosylated pro-Con A) and to other legume lectins. We show here that non-glycosylated pro-Con A expressed in bacteria from recombinant cDNA (rec-pro-Con A) folds in vivo and in vitro to a stable form which is active without further processing. N-glycosylation alone must therefore be sufficient to inactivate pro-Con A--a novel role for glycosylation in regulating activity during protein maturation. |
| Databáze: | OpenAIRE |
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