tailieunhanh - Báo cáo khoa học: Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18

The xylanase inhibitor protein I (XIP-I), recently identified in wheat, inhib-its xylanases belonging to glycoside hydrolase families 10 (GH10) and 11 (GH11). Sequence and structural similarities indicate that XIP-I is related to chitinases of family GH18, despite its lack of enzymatic activity. Here we report the identification and biochemical characterization of a XIP-type inhibitor from rice. | ềFEBS Journal Emergence of a subfamily of xylanase inhibitors within glycoside hydrolase family 18 Anne Durand1 Richard Hughes1 Alain Roussel2 Ruth Flatman1 Bernard Henrissat2 and Nathalie Juge1 3 1 Institute of Food Research IFR Norwich UK 2 Architecture et Fonction des Macromolecules Biologiques UMR6098 CNRS et Universites d Aix-Marseille I et II Marseille France 3 Institut Mediterraneen de Recherche en Nutrition UMR INRA 1111 Faculte des Sciences et Techniques de St Jerome Marseille France Keywords chitinase evolution family 18 glycoside hydrolase proteinaceous xylanase inhibitors rice Present address John Innes Centre Norwich Research Park Colney Norwich NR4 7UH UK Received 16 December 2004 revised 3 February 2005 accepted 9 February 2005 doi The xylanase inhibitor protein I XIP-I recently identified in wheat inhibits xylanases belonging to glycoside hydrolase families 10 GH10 and 11 GH11 . Sequence and structural similarities indicate that XIP-I is related to chitinases of family GH18 despite its lack of enzymatic activity. Here we report the identification and biochemical characterization of a XIP-type inhibitor from rice. Despite its initial classification as a chitinase the rice inhibitor does not exhibit chitinolytic activity but shows specificities towards fungal GH11 xylanases similar to that of its wheat counterpart. This together with an analysis of approximately 150 plant members of glycosidase family GH18 provides compelling evidence that xylanase inhibitors are largely represented in this family and that this novel function has recently emerged based on a common scaffold. The plurifunctionality of GH18 members has major implications for genomic annotations and predicted gene function. This study provides new information which will lead to a better understanding of the biological significance of a number of GH18 inactivated chitinases. Recently two classes of plant proteins designated as XIP xylanase inhibitor protein

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