{Reference Type}: Journal Article
{Title}: Association with Aurora-A Controls N-MYC-Dependent Promoter Escape and Pause Release of RNA Polymerase II during the Cell Cycle.
{Author}: Büchel G;Carstensen A;Mak KY;Roeschert I;Leen E;Sumara O;Hofstetter J;Herold S;Kalb J;Baluapuri A;Poon E;Kwok C;Chesler L;Maric HM;Rickman DS;Wolf E;Bayliss R;Walz S;Eilers M;
{Journal}: Cell Rep
{Volume}: 21
{Issue}: 12
{Year}: Dec 2017 19
暂无{DOI}: 10.1016/j.celrep.2017.11.090
{Abstract}: MYC proteins bind globally to active promoters and promote transcriptional elongation by RNA polymerase II (Pol II). To identify effector proteins that mediate this function, we performed mass spectrometry on N-MYC complexes in neuroblastoma cells. The analysis shows that N-MYC forms complexes with TFIIIC, TOP2A, and RAD21, a subunit of cohesin. N-MYC and TFIIIC bind to overlapping sites in thousands of Pol II promoters and intergenic regions. TFIIIC promotes association of RAD21 with N-MYC target sites and is required for N-MYC-dependent promoter escape and pause release of Pol II. Aurora-A competes with binding of TFIIIC and RAD21 to N-MYC in vitro and antagonizes association of TOP2A, TFIIIC, and RAD21 with N-MYC during S phase, blocking N-MYC-dependent release of Pol II from the promoter. Inhibition of Aurora-A in S phase restores RAD21 and TFIIIC binding to chromatin and partially restores N-MYC-dependent transcriptional elongation. We propose that complex formation with Aurora-A controls N-MYC function during the cell cycle.