The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity

The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex... ATPase/Helicases and nucleases play important roles in DNA end-resection, a critical step during homologous recombination repair in all organisms. In hyperthermophilic archaea the exo-endonuclease NurA and the ATPase HerA cooperate with the highly conserved Mre11-Rad50 complex in 3′ single-stranded DNA (ssDNA) end processing to coordinate repair of double-stranded DNA breaks. Little is known, however, about the assembly mechanism and activation of the HerA-NurA complex. In this study we demonstrate that the NurA exonuclease activity is inhibited by the Sulfolobus solfataricus RecQ-like Hel112 helicase. Inhibition occurs both in the presence and in the absence of HerA, but is much stronger when NurA is in complex with HerA. In contrast, the endonuclease activity of NurA is not affected by the presence of Hel112. Taken together these results suggest that the functional interaction between NurA/HerA and Hel112 is important for DNA end-resection in archaeal homologous recombination. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Extremophiles Springer Journals

The Sulfolobus solfataricus RecQ-like DNA helicase Hel112 inhibits the NurA/HerA complex exonuclease activity

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Publisher
Springer Journals
Copyright
Copyright © 2018 by Springer Japan KK, part of Springer Nature
Subject
Life Sciences; Microbiology; Biotechnology; Biochemistry, general; Microbial Ecology
ISSN
1431-0651
eISSN
1433-4909
D.O.I.
10.1007/s00792-018-1018-7
Publisher site
See Article on Publisher Site

Abstract

ATPase/Helicases and nucleases play important roles in DNA end-resection, a critical step during homologous recombination repair in all organisms. In hyperthermophilic archaea the exo-endonuclease NurA and the ATPase HerA cooperate with the highly conserved Mre11-Rad50 complex in 3′ single-stranded DNA (ssDNA) end processing to coordinate repair of double-stranded DNA breaks. Little is known, however, about the assembly mechanism and activation of the HerA-NurA complex. In this study we demonstrate that the NurA exonuclease activity is inhibited by the Sulfolobus solfataricus RecQ-like Hel112 helicase. Inhibition occurs both in the presence and in the absence of HerA, but is much stronger when NurA is in complex with HerA. In contrast, the endonuclease activity of NurA is not affected by the presence of Hel112. Taken together these results suggest that the functional interaction between NurA/HerA and Hel112 is important for DNA end-resection in archaeal homologous recombination.

Journal

Extremophiles – Springer Journals

Published: Feb 27, 2018

References

  • Mechanistic insight into the assembly of the HerA-NurA helicase-nuclease DNA end resection complex
    Ahdash, Z
  • At loose ends: resecting a double-strand break
    Bernstein, KA; Rothstein, R
  • Structural and functional insights into DNA-end processing by the archaeal HerA helicase-NurA nuclease complex
    Blackwood, JK
  • Roles of DNA helicases in the maintenance of genome integrity
    Bochman, ML
  • Relationship of DNA degradation by Saccharomyces cerevisiae exonuclease 1 and its stimulation by RPA and Mre11-Rad50-Xrs2 to DNA end resection
    Cannavo, E
  • DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2
    Cejka, P
  • Crystal structure of the NurA-dAMP-Mn2+ complex
    Chae, J
  • Playing the end game: DNA double-strand break repair pathway choice
    Chapman, JR
  • Biochemical and functional characterization of the NurA-HerA complex from Deinococcus radiodurans
    Cheng, K
  • NurA, a novel 5′-3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea
    Constantinesco, F
  • A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
    Constantinesco, F
  • NurA is endowed with endo- and exonuclease activities that are modulated by HerA: new insight into their role in DNA-End processing
    Falco, M
  • A novel DNA helicase with strand-annealing activity from the crenarchaeon Sulfolobus solfataricus
    Felice, M
  • Mre11-Rad50 promotes rapid repair of DNA damage in the polyploid archaeon Haloferax volcanii by restraining homologous recombination
    Delmas, S
  • Response of the hyperthermophilic archaeon Sulfolobus solfataricus to UV damage
    Frols, S
  • Genetic analysis of DNA repair in the hyperthermophilic archaeon, Thermococcus kodakaraensis
    Fujikane, R
  • DNA helicases Sgs1 and BLM promote DNA double-strand break resection
    Gravel, S
  • RecA family proteins in archaea: RadA and its cousins
    Haldenby, S
  • Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine
    Hopfner, KP
  • The P. furiosus mre11/rad50 complex promotes 5′ strand resection at a DNA double-strand break
    Hopkins, BB; Paull, TT
  • Comparative genomics of the FtsK-HerA superfamily of pumping ATPases: implications for the origins of chromosome segregation, cell division and viral capsid packaging
    Iyer, LM
  • Anomalous electrophoretic migration of short oligodeoxynucleotides labelled with 5′-terminal Cy5 dyes
    Killelea, T
  • Rad50 is not essential for the Mre11-dependent repair of DNA double-strand breaks in Halobacterium sp. strain NRC-1
    Kish, A; DiRuggiero, J
  • Initiation of genetic recombination and recombination-dependent replication
    Kowalczykowski, SC
  • Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex
    Lengsfeld, BM
  • The archaeal Xpf/Mus81/FANCM homolog Hef and the Holliday junction resolvase Hjc define alternative pathways that are essential for cell viability in Haloferax volcanii
    Lestini, R
  • Hjm/Hel308A DNA helicase from Sulfolobus tokodaii promotes replication fork regression and interacts with Hjc endonuclease in vitro
    Li, Z
  • Knockouts of RecA-like proteins RadC1 and RadC2 have distinct responses to DNA damage agents in Sulfolobus islandicus
    Liang, PJ
  • Structure and function of nucleases in DNA repair: shape, grip and blade of the DNA scissors
    Lindahl, T; Wood, RD
  • Mechanisms and regulation of DNA end resection
    Longhese, MP
  • Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing
    Mimitou, EP; Symington, LS
  • DNA end resection: many nucleases make light work
    Mimitou, EP; Symington, LS
  • Mre11-Rad50-Xrs2 and Sae2 promote 5′ strand resection of DNA double-strand breaks
    Nicolette, ML
  • BLM-DNA2-RPA-MRN and EXO1-BLM-RPA-MRN constitute two DNA end resection machineries for human DNA break repair
    Nimonkar, AV
  • Quality control by DNA repair
    Nishino, T; Morikawa, K
  • Mechanism of the ATP-dependent DNA end-resection machinery from Saccharomyces cerevisiae
    Niu, H
  • The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius
    Quaiser, A
  • DNA polymerase lambda from calf thymus preferentially replicates damaged DNA
    Ramadan, K
  • Structure of the DNA repair helicase Hel308 reveals DNA binding and autoinhibitory domains
    Richards, JD
  • Repair of DNA double-strand breaks following UV damage in three Sulfolobus solfataricus strains
    Rolfsmeier, ML
  • Synergic and opposing activities of thermophilic RecQ-like helicase and topoisomerase 3 proteins in Holliday junction processing and replication fork stabilization
    Valenti, A
  • Physical and functional interaction between archaeal single-stranded DNA-binding protein and the 5′-3′ nuclease NurA
    Wei, T
  • Molecular biology of Hel308 helicase in archaea
    Woodman, IL; Bolt, EL
  • Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates
    Zhang, S
  • Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
    Zhu, Z

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