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Molecular Biology and Evolution, Vol 13, 990-998, Copyright © 1996 by Society for Molecular Biology and Evolution

ORIGINAL ARTICLE

The divergent domains of the NEFA and nucleobindin proteins are derived from an EF-hand ancestor

A Karabinos, D Bhattacharya, C Morys-Wortmann, K Kroll, G Hirschfeld, HD Kratzin, S Barnikol-Watanabe and N Hilschmann
Department of Immunochemistry, Max Planck Institute for Experimental Medicine, Gottingen, Germany.

The human protein NEFA (DNA binding, EF-hand, Acidic region) has previously been isolated from a KM3 cell line and immunolocalized on the plasma membrane, in the cytoplasma, and in the culture medium. Sequence analysis of a cDNA clone encoding NEFA identified a hydrophilic domain, two EF-hands, and a leucine zipper at the C- terminus. These characters are shared with nucleobindin (Nuc). In this paper we have further characterized NEFA and probed its evolutionary origins. Circular dichroism (CD) spectra of recombinant NEFA indicated a helical content of 51% and showed that the EF-hands are capable of binding Ca2+. Experiments with recombinant NEFA and synthesized peptides revealed that the leucine zipper cannot form a homodimer. The leucine zipper may allow heterodimer formation of NEFA and an unknown protein. Phylogenetic analyses suggest that this protein is derived from a four-domain EF-hand ancestor with subsequent duplications and fusions. The leucine zipper and putative DNA-binding domains of NEFA have evolved secondarily from existing EF-hand sequences. These analyses provide insights into how complex proteins may originate and trace the precursor of NEFA to the common ancestor of eukaryotes.
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