Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage.
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.
Min
W
W
Molecular Biology Research Group, School of Biological Sciences, University College of Swansea, Wales, UK.
Dunn
A J
AJ
Jones
D H
DH
D001483:Base Sequence; D002846:Chromatography, Affinity / Q000379:methods; D003001:Cloning, Molecular; D003208:Concanavalin A / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D007887:Fabaceae / Q000235:genetics*; D006031:Glycosylation; D008958:Models, Molecular; D008969:Molecular Sequence Data; D008970:Molecular Weight; D037121:Plant Lectins; D010946:Plants, Medicinal; D011487:Protein Conformation; D011498:Protein Precursors / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
D037121:Plant Lectins; D011498:Protein Precursors; D021382:Protein Sorting Signals; D011994:Recombinant Proteins; C074083:pro-concanavalin A; D003208:Concanavalin A