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Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage.

ABSTRACT: HLTF is a pivotal protein in the template-switching pathway that allows DNA synthesis to continue even in the presence of DNA damage by utilizing a newly synthesized undamaged strand as a template. HLTF has a novel DNA-binding domain termed HIRAN that has been recently found in various proteins, although its detailed function remains unclear. In this study, the HIRAN domain of human HLTF was successfully crystallized. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 130.0, c = 150.1 Å.

SUBMITTER: Ikegaya Y

PROVIDER: S-EPMC4461327 | biostudies-other | 2015 Jun

REPOSITORIES: biostudies-other

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Crystallographic study of a novel DNA-binding domain of human HLTF involved in the template-switching pathway to avoid the replication arrest caused by DNA damage.

Ikegaya Yuzu Y Hara Kodai K Hishiki Asami A Yokoyama Hideshi H Hashimoto Hiroshi H

Acta crystallographica. Section F, Structural biology communications 20150520 Pt 6

HLTF is a pivotal protein in the template-switching pathway that allows DNA synthesis to continue even in the presence of DNA damage by utilizing a newly synthesized undamaged strand as a template. HLTF has a novel DNA-binding domain termed HIRAN that has been recently found in various proteins, although its detailed function remains unclear. In this study, the HIRAN domain of human HLTF was successfully crystallized. The crystals belonged to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell ...[more]

PMID: 26057792

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