In Vivo Chaperone-Assisted Folding of α-1,6-Fucosyltransferase from Rhizobium sp.

3 pages, 3 figures.-- PMID: 12794864 [PubMed].-- Supplementary information (Materials and methods, 8 pages) available at: http://www.wiley-vch.de/contents/jc_2268/2003/z514_s.pdfGlycosyltransferases have become powerful tools for the synthesis of oligosaccharides through their strict control over the stereo- and regioselectivity of glycosidic bond formation. One major drawback of glycosyltransferases in synthesis is their limited availability. The cloning and overexpression of bacterial glycosyltransferases is one alternative to overcome this problem. However, when a heterologous protein is over-expressed in E. coli misfolding and aggregation happen frequently, driving the recombinant protein into inactive aggregates known as inclusion bodies (I.B.). One possible and attractive strategy to avoid their formation is to increase the cellular levels of molecular chaperones. Chaperonins are able to mediate ATP-dependent folding of polypeptides to the native state. GroEL from E. coli is the best characterized chaperonin and its function is dependent on the cochaperonin GroES.A.B was supported by a postdoctoral I3P contract of the European Social Found. This work was supported by the Spanish DGI (Grants BQU2001-1503 and PTR1995-0568-OP).Peer reviewe