%0 Journal Article
%T Association with Aurora-A Controls N-MYC-Dependent Promoter Escape and Pause Release of RNA Polymerase II during the Cell Cycle.
%A Büchel G
%A Carstensen A
%A Mak KY
%A Roeschert I
%A Leen E
%A Sumara O
%A Hofstetter J
%A Herold S
%A Kalb J
%A Baluapuri A
%A Poon E
%A Kwok C
%A Chesler L
%A Maric HM
%A Rickman DS
%A Wolf E
%A Bayliss R
%A Walz S
%A Eilers M
%J Cell Rep
%V 21
%N 12
%D Dec 2017 19
%M 29262328
暂无%R 10.1016/j.celrep.2017.11.090
%X 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.