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Title
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Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage.
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Authors
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W.Min,
A.J.Dunn,
D.H.Jones.
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Ref.
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Embo J, 1992,
11,
1303-1307.
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PubMed id
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Abstract
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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.
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