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PDBsum entry 6kcs
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DNA binding protein/DNA
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PDB id
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6kcs
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References listed in PDB file
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Key reference
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Title
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Structure of hiran domain of human hltf bound to duplex DNA provides structural basis for DNA unwinding to initiate replication fork regression.
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Authors
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A.Hishiki,
M.Sato,
H.Hashimoto.
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Ref.
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J Biochem, 2020,
167,
597-602.
[DOI no: ]
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PubMed id
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Abstract
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Replication fork regression is a mechanism to rescue a stalled fork by various
replication stresses, such as DNA lesions. Helicase-like transcription factor, a
SNF2 translocase, plays a central role in the fork regression and its N-terminal
domain, HIRAN (HIP116 and Rad5 N-terminal), binds the 3'-hydroxy group of
single-stranded DNA. Furthermore, HIRAN is supposed to bind double-stranded DNA
(dsDNA) and involved in strand separation in the fork regression, whereas
structural basis for mechanisms underlying dsDNA binding and strand separation
by HIRAN are still unclear. Here, we report the crystal structure of HIRAN bound
to duplex DNA. The structure reveals that HIRAN binds the 3'-hydroxy group of
DNA and unexpectedly unwinds three nucleobases of the duplex. Phe-142 is
involved in the dsDNA binding and the strand separation. In addition, the
structure unravels the mechanism underlying sequence-independent recognition for
purine bases by HIRAN, where the N-glycosidic bond adopts syn conformation. Our
findings indicate direct involvement of HIRAN in the fork regression by
separating of the daughter strand from the parental template.
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