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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper.

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.[1]

References

  1. A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper. Acker, J., Wintzerith, M., Vigneron, M., Kedinger, C. DNA Seq. (1994) [Pubmed]
 
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