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M211834200v1
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Papers In Press, published online ahead of print February 4, 2003
J. Biol. Chem, 10.1074/jbc.M211834200
Submitted on November 20, 2002
Revised on February 4, 2003
Accepted on February 4, 2003

Identification of an archaeal alpha -L-fucosidase encoded by an interrupted gene: production of a functional enzyme by mutations mimicking programmed -1 frameshifting

Beatrice Cobucci-Ponzano, Antonio Trincone, Assunta Giordano, Mose' Rossi, and Marco Moracci

Institute of Protein Biochemistry, Consiglio Nazionale delle Ricerche, Naples 80131

Corresponding Author: moracci{at}dafne.ibpe.na.cnr.it

The analysis of the complete genome of the thermoacidophilic Archaeon Sulfolobus solfataricus revealed two open reading frames (ORF)1, named SSO11867 and SSO3060, interrupted by a -1 frameshift and encoding for the N- and the C-terminal fragments, respectively, of an alpha -L-fucosidase. We report here that these ORFs are actively transcribed in vivo, and we confirm the presence of the -1 frameshift between them at cDNA level, explaining why we could not find alpha -fucosidase activity in S. solfataricus extracts. Detailed analysis of the region of overlap between the two ORFs revealed the presence of the consensus sequence for a programmed -1 frameshifting. Two specific mutations, mimicking this regulative frameshifting event, allow the expression, in E. coli, of a fully active thermophilic and thermostable alpha -L-fucosidase (EC 3.2.1.51) with micro-molar substrate specificity and showing transfucosylating activity. The analysis of the fucosylated products of this enzyme allows, for the first time, to assign a retaining reaction mechanism to family 29 of glycosyl hydrolases. The presence of an alpha -fucosidase putatively regulated by programmed -1 frameshifting is intriguing both with respect to the regulation of gene expression and, in post-genomic era, for the definition of gene function in Archaea.


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