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Título

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

AutorBastida, Agatha; Latorre, Montserrat; García-Junceda, Eduardo
Palabras claveChaperone proteins
Gene expression
Glycosyltransferases
Immobilization
Protein folding
Fecha de publicación3-jun-2003
EditorJohn Wiley & Sons
CitaciónChemBioChem 4(6): 531-533 (2003)
ResumenGlycosyltransferases 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.
Descripción3 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.pdf
Versión del editorhttp://dx.doi.org/10.1002/cbic.200200514
URIhttp://hdl.handle.net/10261/10670
DOI10.1002/cbic.200200514
ISSN1439-4227
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