Identification of a Substrate Recognition Domain in the Replication Stress Response Protein Zinc Finger Ran-binding Domain-containing Protein 3 (ZRANB3).

Badu-Nkansah A, Mason AC, Eichman BF, Cortez D
J Biol Chem. 2016 291 (15): 8251-7

PMID: 26884333 · PMCID: PMC5414104 · DOI:10.1074/jbc.M115.709733

DNA damage and other forms of replication stress can cause replication forks to stall. Replication stress response proteins stabilize and resolve stalled forks by mechanisms that include fork remodeling to facilitate repair or bypass of damaged templates. Several enzymes including SMARCAL1, HLTF, and ZRANB3 catalyze these reactions. SMARCAL1 and HLTF utilize structurally distinct accessory domains attached to an ATPase motor domain to facilitate DNA binding and catalysis of fork remodeling reactions. Here we describe a substrate recognition domain within ZRANB3 that is needed for it to recognize forked DNA structures, hydrolyze ATP, catalyze fork remodeling, and act as a structure-specific endonuclease. Thus, substrate recognition domains are a common feature of fork remodeling, SNF2-family, DNA-dependent ATPases, and our study provides further mechanistic understanding of how these enzymes maintain genome integrity during DNA replication.

© 2016 by The American Society for Biochemistry and Molecular Biology, Inc.

MeSH Terms (13)

Adenosine Triphosphate Amino Acid Sequence Animals DNA DNA Damage DNA Helicases DNA Repair HEK293 Cells Humans Mice Molecular Sequence Data Protein Structure, Tertiary Sequence Alignment

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