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A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper
J Acker1, M Wintzerith, M Vigneron
1Laboratoire de Génétique Moléculaire des Eucaryotes (CNRS), Unité 184 de Biologie Moléculaire et de Génétique (INSERM), Institut de Chime Biologique de la Faculté de Médecine, Strasbourg, France.
Abstract:
The cDNA of a small subunit (hRPB14.4) of RNA polymerase II (or B) from HeLa cells has been cloned. A 127 residue peptide sequence (calculated molecular weight of 14,478; isoelectric point of 3.7) was deduced and compared to that of the homologous subunit of Saccharomyces cerevisiae polymerase (ABC23, encoded by the RPB6/RPO26 gene). About 50% of the total residues were found to be conserved between yeast and man, with the C-terminal two-third being the most conserved (72% identity). A putative leucine-zipper comprising four properly spaced leucine residues, but not preceded by a basic domain, was identified near the C-terminal end of both proteins.