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Papers In Press, published online ahead of print July 2, 2001
J. Biol. Chem, 10.1074/jbc.M105303200
Submitted on June 8, 2001
Revised on July 2, 2001
Accepted on June 29, 2001
Clare Hall Laboratories, Imperial Cancer Research Fund, South Mimms, Herts EN6 3LD
Corresponding Author: j.svejstrup{at}icrf.icnet.uk
Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity-chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the previously identified Elp1, Elp2, and Elp3 proteins, and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.
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