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Nucleic Acids Research, 1993, Vol. 21, No. 18 4218-4225
© 1993

MOLECULAR BIOLOGY

RNA binding properties and evoultionary conservation of the Xenopus multifinger protein Xfin

Massimiliano Andreazzoli, Stefania De Lucchini*, Mario costa1 and Giuseppina Barsacchi

Laboratorid di Biologia Cellulare e dello Sviluppo, dipartimento di Fisiologia e Biochimica, Universita' di Pisa Via Carducci 13, 56010 Ghezzano, Pisa 1Istituto di Farmacologia Medica Universita' di pisa Via Roma 55, 56100 Pisa, Italy

*To whom correspondence should be addressed

Received June 14, 1993. Accepted August 10, 1993.

Xfin Is a Xenopus zinc finger protein which is expressed in the cytoplasm of the oocyte and throughout embryogenesis, as well as in the cytoplasm of some specific and highly differentiated cell types (De Lucchini et al., Mech. Dev. 36, 31 – 4 0 , 1991). In this paper we present a characterization of some structural features of the protein and of Its nucleic acid binding properties. We found that Xfln is a phosphoprotein, Is present in the soluble fraction of the cytoplasm, and Is actively phosphorylated in cytosollc extracts. Several putative phosphorylatlon sites are present in the cDNA-derived protein sequence, mostly located at specific positions within the Zn-flngers. In an In vitro assay a fusion protein containing part of the finger region of Xfln exhibits specific binding to a poly (G) RNA homopolymer, while it does not bind DNA. The RNA binding activity of the protein is significantly enhanced by phosphorylatlon. A putative Xfln homolog, which appears to be evolutionary conserved with regard to size, cytoplasmlc expression and antigenlc specificity, is present in representatives of five Vertebrate classes. Taken together, these results may suggest that, by virtue of its RNA binding activity modulated through phosphorylation, Xfln could serve some evolutionary conserved function in post-transcriptlonal regulation processes.


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