Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin.

Sandro Holzer, Gianluca Degliesposti, Mairi L Kilkenny, Sarah L Maslen, Dijana Matak-Vinkovíc, Mark Skehel, Luca Pellegrini

Nucleic acids research 2017 May 19

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Human Timeless is involved in replication fork stabilization, S-phase checkpoint activation and establishment of sister chromatid cohesion. In the cell, Timeless forms a constitutive heterodimeric complex with Tipin. Here we present the 1.85 Å crystal structure of a large N-terminal segment of human Timeless, spanning amino acids 1-463, and we show that this region of human Timeless harbours a partial binding site for Tipin. Furthermore, we identify minimal regions of the two proteins that are required for the formation of a stable Timeless-Tipin complex and provide evidence that the Timeless-Tipin interaction is based on a composite binding interface comprising different domains of Timeless. © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

Citation

Sandro Holzer, Gianluca Degliesposti, Mairi L Kilkenny, Sarah L Maslen, Dijana Matak-Vinkovíc, Mark Skehel, Luca Pellegrini. Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin. Nucleic acids research. 2017 May 19;45(9):5555-5563