The Archaeal ATPase PINA Interacts with the Helicase Hjm Via Its Carboxyl Terminal KH Domain Remodeling and Processing Replication Fork and Holliday Junction

Overview

Journal Nucleic Acids Res

Publisher Oxford University Press

Specialty Biochemistry

Date 2018 May 31

PMID 29846688

Citations 6

Authors

Binyuan Zhai

Kevin DuPrez

Xiaoyun Han

Zenglin Yuan

Sohail Ahmad

Cheng Xu

Lichuan Gu

Jinfeng Ni

Li Fan

Yulong Shen

Affiliations

Soon will be listed here.

Abstract

PINA is a novel ATPase and DNA helicase highly conserved in Archaea, the third domain of life. The PINA from Sulfolobus islandicus (SisPINA) forms a hexameric ring in crystal and solution. The protein is able to promote Holliday junction (HJ) migration and physically and functionally interacts with Hjc, the HJ specific endonuclease. Here, we show that SisPINA has direct physical interaction with Hjm (Hel308a), a helicase presumably targeting replication forks. In vitro biochemical analysis revealed that Hjm, Hjc, and SisPINA are able to coordinate HJ migration and cleavage in a concerted way. Deletion of the carboxyl 13 amino acid residues impaired the interaction between SisPINA and Hjm. Crystal structure analysis showed that the carboxyl 70 amino acid residues fold into a type II KH domain which, in other proteins, functions in binding RNA or ssDNA. The KH domain not only mediates the interactions of PINA with Hjm and Hjc but also regulates the hexameric assembly of PINA. Our results collectively suggest that SisPINA, Hjm and Hjc work together to function in replication fork regression, HJ formation and HJ cleavage.

Citing Articles

Evolutionary and functional insights into the Ski2-like helicase family in Archaea: a comparison of Thermococcales ASH-Ski2 and Hel308 activities.

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Archaeal Hel308 suppresses recombination through a catalytic switch that controls DNA annealing.

Lever R, Simmons E, Gamble-Milner R, Buckley R, Harrison C, Parkes A Nucleic Acids Res. 2023; 51(16):8563-8574.

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Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase.

Hajj M, Langendijk-Genevaux P, Batista M, Quentin Y, Laurent S, Capeyrou R Biomolecules. 2021; 11(7).

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The KH domain facilitates the substrate specificity and unwinding processivity of DDX43 helicase.

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