CPF1 PROTEIN-INDUCED BENDING OF YEAST CENTROMERE DNA ELEMENT-1

The centromere complex is a multicomponent structure essential for fai thful chromosome transmission. Here we show that the S.cerevisiae cent romere protein Cpf1 bends centromere DNA element I (CDEI) with the ben d angle ranging from 66-degrees to 71-degrees. CDEI DNA sequences that carry point mutations which lead to reduced Cpf1 binding affinity and in vivo centromere activity are still able to show bending. The Cpf1 induced bend is directed towards the major groove with the bend centre located in CDEI. An intrinsic bend cannot replace the Cpf1 induced DN A bend for in vivo centromere function. An in vivo phasing experiment suggests that both the distance and the correct spatial arrangement of the CDEI/Cpf1 complex to CDEII and CDEIII are important for optimal c entromere function.