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Vol. 273, Issue 3, 1634-1639, January 16, 1998

NA14 Is a Novel Nuclear Autoantigen with a Coiled-coil Domain

Francisco Ramos-Morales, Carlos Infante, Concepción Fedriani, Michel Bornens^**, and Rosa M. Rios^**

From the  Departamento de Microbiología, Facultad de Biología, Universidad de Sevilla, Apdo. 1095, 41080 Sevilla, Spain and the ^** Institut Curie, Section Recherche, UMR 144 du CNRS, 26 rue d'Ulm, 75248 Paris, Cedex 05, France

The serum from a patient with Sjögren's syndrome (RM serum) was used to screen a human testis cDNA expression library. A cDNA of 865 base pairs containing the entire coding sequence for a novel protein was isolated. The 14-kDa predicted protein contains an acidic domain (amino acids 6-80) with a high frequency of heptad repeats characteristic of -helices that form dimeric coiled-coil structures and an alkaline carboxyl-terminal domain (amino acids 81-119). It seems to be widely expressed, but its expression level varies depending on tissues. A protein of apparent molecular mass of 14 kDa was immunoprecipitated from cell lysates by the autoimmune serum, and it was recognized by rabbit antibodies raised to a recombinant bacterial fusion protein generated from the cDNA clone. Conventional and confocal immunofluorescence microscopy on HeLa and 3T3 cells transiently transfected with a tagged form of the protein showed numerous punctate structures scattered throughout the nucleus. This novel protein has been termed NA14 for Nuclear Autoantigen of 14 kDa.

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