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

DOI: 10.1093/nar/gkx139 DOI Help

Authors: Sandro Holzer (University of Cambridge) , Gianluca Degliesposti (MRC Laboratory of Molecular Biology) , Mairi L. Kilkenny (University of Cambridge) , Sarah L. Maslen (MRC Laboratory of Molecular Biology) , Dijana Matak-vinkovíc (University of Cambridge) , Mark Skehel (MRC Laboratory of Molecular Biology) , Luca Pellegrini (University of Cambridge)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nucleic Acids Research

State: Published (Approved)
Published: February 2017
Diamond Proposal Number(s): 9537

Open Access Open Access

Abstract: 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.

Journal Keywords: amino acids; binding sites; chromatids; s phase; dna replication fork; cell cycle checkpoint; crystal structure

Subject Areas: Medicine, Biology and Bio-materials, Chemistry


Instruments: I02-Macromolecular Crystallography

Documents:
gkx139.pdf