RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes
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RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes. / Sebastiaan Winkler, G.; Petrakis, Thodoris G.; Ethelberg, Steen; Tokunaga, Masao; Erdjument-Bromage, Hediye; Tempst, Paul; Svejstrup, Jesper Q.
In: Journal of Biological Chemistry, Vol. 276, No. 35, 31.08.2001, p. 32743-32749.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes
AU - Sebastiaan Winkler, G.
AU - Petrakis, Thodoris G.
AU - Ethelberg, Steen
AU - Tokunaga, Masao
AU - Erdjument-Bromage, Hediye
AU - Tempst, Paul
AU - Svejstrup, Jesper Q.
PY - 2001/8/31
Y1 - 2001/8/31
N2 - 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.
AB - 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.
U2 - 10.1074/jbc.M105303200
DO - 10.1074/jbc.M105303200
M3 - Journal article
C2 - 11435442
AN - SCOPUS:0035980015
VL - 276
SP - 32743
EP - 32749
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 35
ER -
ID: 331575710