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Non-glycosylated recombinant pro-concanavalin A is active without polypeptide cleavage
1Molecular Biology Research Group, School of Biological Sciences, University College of Swansea, Wales, UK.
The EMBO Journal
|April 1, 1992
Summary
Concanavalin A (Con A) undergoes unique circular permutation during maturation. This study reveals that N-glycosylation alone inactivates the precursor, a novel regulatory role for glycosylation in protein processing.
Area of Science:
- Biochemistry
- Plant Molecular Biology
- Protein Chemistry
Background:
- Concanavalin A (Con A) is a legume lectin with a complex maturation process.
- Mature Con A exhibits circular permutation in its primary sequence compared to its precursor and other lectins.
- The role of glycosylation in Con A precursor inactivation is not fully understood.
Purpose of the Study:
- To investigate the role of N-glycosylation in the post-translational processing and activity of concanavalin A.
- To determine if the inactive precursor form of Con A (pro-Con A) can be activated without further processing.
- To elucidate the mechanism by which glycosylation regulates Con A activity.
Main Methods:
- Expression of non-glycosylated pro-Con A in bacteria using recombinant cDNA.
- In vitro and in vivo folding studies of recombinant pro-Con A.
- Assessment of the biological activity of the folded recombinant pro-Con A.
Main Results:
- Non-glycosylated pro-Con A, expressed recombinantly, folds into a stable and active form.
- This active form does not require further processing for Con A activity.
- N-glycosylation is demonstrated to be sufficient for inactivating pro-Con A.
Conclusions:
- N-glycosylation plays a critical role in regulating concanavalin A activity during protein maturation.
- The inactivation of pro-Con A by N-glycosylation is a novel finding in protein regulation.
- This suggests glycosylation can act as a direct switch for protein function.