Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin. Issue 9 (25th February 2017)

• Record Type: Journal Article
• Authors: Holzer, Sandro; Degliesposti, Gianluca; Kilkenny, Mairi L; Maslen, Sarah L; Matak-Vinkovíc, Dijana; Skehel, Mark; Pellegrini, Luca
• Is Part Of: Nucleic acids research. Volume 45:Issue 9(2017)
• Page Start: 5555
• Page End: 5563
• Publication Date: 2017-02-25
• Subjects: Nucleic acids -- Periodicals; Molecular biology -- Periodicals; 572.805
• DOI: 10.1093/nar/gkx139
• Languages: English
• ISSNs: 0305-1048

Abstract

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.