Min W, Dunn A J, Jones D H
Molecular Biology Research Group, School of Biological Sciences, University College of Swansea, Wales, UK.
EMBO J. 1992 Apr;11(4):1303-7. doi: 10.1002/j.1460-2075.1992.tb05174.x.
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.
