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Nucleic Acids Research, 2002, Vol. 30, No. 16 3592-3601
© 2002 Oxford University Press

Metallo-ß-lactamase fold within nucleic acids processing enzymes: the ß-CASP family

Isabelle Callebaut*, Despina Moshous1, Jean-Paul Mornon and Jean-Pierre de Villartay1

Systèmes moléculaires et Biologie structurale, LMCP, CNRS UMR 7590, Universités Paris 6 et Paris 7, case 115, 4 place Jussieu, F-75252 Paris Cedex 05, France and 1 Développement Normal et Pathologique du Système Immunitaire, INSERM U429, Hôpital Necker Enfants Malades, 149 rue de Sèvres, F-75015 Paris, France

*To whom correspondence should be addressed. Tel: +33 1 44 27 45 87; Fax: +33 1 44 27 37 85; Email: isabelle.callebaut{at}lmcp.jussieu.fr

A separate family of enzymes within the metallo-ß-lactamase fold comprises several important proteins acting on nucleic acid substrates, involved in DNA repair (Artemis, SNM1 and PSO2) and RNA processing [cleavage and polyadenylation specificity factor (CPSF) subunit]. Proteins of this family, named ß-CASP after the names of its representative members, possess specific features relative to those of other metallo-ß-lactamases, that are concentrated in the C-terminal part of the domain. In this study, using sensitive methods of sequence analysis, we identified highly conserved amino acids specific to the ß-CASP family, some of which were unidentified to date, that are predicted to play critical roles in the enzymatic function. The identification and characterisation of all the extant, detectable ß-CASP members within sequence databases and genome data also allowed us to unravel particular sequence features which are likely to be involved in substrate specificity, as well as to describe new but as yet uncharacterised members which may play critical roles in DNA and RNA metabolism.


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