Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4

Abstract

for the first time. These observations lead to a mechanism of RapAmediated RNAP recycling, including the RapA-facilitated release of sequestered RNAP from DNA template and the 70-dependent removal of RapA from the RapACORE complex for transcription reinitiation. The derived mechanism of RapA provides a framework for further structural and biochemical investigations on, for example, how and where RNAP becomes sequestered in the PTC, the exact composition of the PTC, the DNA translocase activity of RapA and its precise mechanism, and additional factors that may contribute to the destabilization of the PTC.