Abstract

Chromatin remodeler Chd1 is one of the major types of ATP driven motor protein which moves along DNA, gaining energy from ATP hydrolysis and uses DNA as a ‘Rail’ to promote gene transcription by moving or ejecting the nucleosome. However, the motor mechanism by which this is done is still obscure at molecular level. In our study, we analyzed the properties of the Chd1-ADP-Pi analogues ternary complexes which mimic transient states in ATPase cycle for both the full length CHD1 (CHD1-FL) and catalytical motor domain of CHD1 (CHD1-MD) in order to clarify how ATP chemical energy transduced to motor activity.

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