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

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.

SUBMITTER: Holzer S

PROVIDER: S-EPMC5605233 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature

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

Holzer Sandro S Degliesposti Gianluca G Kilkenny Mairi L ML Maslen Sarah L SL Matak-Vinkovíc Dijana D Skehel Mark M Pellegrini Luca L

Nucleic acids research 20170501 9

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 r ...[more]

PMID: 28334766

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