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

Falco, Mariarosaria De; Massa, Federica; Rossi, Mosè; Felice, Maurilio De

doi:10.1007/s00792-018-1018-7

Cited by 5 publications

(8 citation statements)

References 45 publications

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“…While there is much that remains to be uncovered with respect to the cellular functions of aLhr2 in vivo, we can propose the following roles for Thermococcales aLhr2. First, the detection of Paby-aLhr2 in the interaction network of the replication protein A complex (RPA) [19] is consistent with studies proposing that aLhr2 helicases are involved in DNA recombination and repair in S. solfataricus and M. thermautotrophicus [15,41]. Indeed, RPA that binds ssDNA is crucial for both DNA replication and DNA damage response [47].…”

Section: Discussionsupporting

confidence: 77%

“…We showed that Tbar-aLhr2 is a nucleic acid-dependent ATPase with no preference for DNA or RNA molecules ( Figure 5). Only, the archaeal Ssol-aLhr2 was shown to be able to hydrolyse ATP in absence of nucleic acids [41]. Ssol-aLhr2 also differs from the monomeric Tbar-aLhr2 and bacterial Lhr proteins by its low affinity for single-stranded DNA and by its oligomeric state that can be both monomeric and dimeric; monomers and dimers having specific biochemical activities.…”

Section: Discussionmentioning

confidence: 98%

“…We determined that it is a monomeric DNA/RNA helicase able to process DNA:RNA and RNA:RNA duplexes. Moreover, for other archaeal aLhr helicases that were proposed to be DNA helicases involved in DNA repair and recombination [15,41], it was unclear if they belong to the same aLhr2 group. It also interrogated the relationship that exists between the archaeal and bacterial Lhr proteins.…”

Section: Discussionmentioning

confidence: 99%

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

Hajj¹,

Langendijk-Genevaux²,

Batista³

et al. 2021

Preprint

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Helicases are proteins that use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of the DNA and RNA metabolisms and participate in numerous repair mechanisms that maintain cellular integrity. Helicases are classified into 6 superfamilies (SF1-6). The archaeal Lhr-type proteins are SF2 helicases that are mostly uncharacterized. They have been proposed to be a DNA helicase that acts in DNA recombination and repair processes in Sulfolobales and Methanothermobacter. In parallel, a protein annotated as an Lhr2 protein was also found in the network of proteins involved in RNA metabolism in Thermococcales. To this respect, we performed in-depth phylogenomic analyses to report the classification and taxonomic distribution of Lhr-type proteins in Archaea, and to better understand their relationship with bacterial Lhr. Furthermore, with the goal of envisioning the role(s) of aLhr2 in archaeal cells, we deciphered the enzymatic activities of aLhr2 from Thermococcus barophilus (Tbar). We showed that Tbar-aLhr2 is a DNA/RNA helicase acting on DNA:RNA and RNA:RNA duplexes and proposed that aLhr2 helicases are involved in processes dependent of DNA and RNA transactions.

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Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

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

Hajj¹,

Langendijk-Genevaux²,

Batista³

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

“…We showed that Tbar-aLhr2 is a nucleic acid-dependent ATPase with no apparent preference for DNA or RNA molecules (Figure 5). Only the archaeal Ssol-aLhr2 was shown to be able to hydrolyse ATP in the absence of nucleic acids [41]. Ssol-aLhr2 also differs from the monomeric Tbar-aLhr2 and bacterial Lhr proteins by its low affinity for single-stranded DNA and by its oligomeric state that can be both monomeric and dimeric; monomers and dimers having specific biochemical activities.…”

Section: Discussionmentioning

confidence: 99%

“…We determined that it is a monomeric DNA/RNA helicase able to process DNA:RNA and RNA:RNA duplexes. Moreover, for other archaeal aLhr helicases that were proposed to be DNA helicases involved in DNA repair and recombination [15,41], it was unclear if they belonged to the same aLhr2 group. We also interrogated the relationship that exists between the archaeal and bacterial Lhr proteins.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2021

View full text Add to dashboard Cite

Helicase proteins are known to use the energy of ATP to unwind nucleic acids and to remodel protein-nucleic acid complexes. They are involved in almost every aspect of DNA and RNA metabolisms and participate in numerous repair mechanisms that maintain cellular integrity. The archaeal Lhr-type proteins are SF2 helicases that are mostly uncharacterized. They have been proposed to be DNA helicases that act in DNA recombination and repair processes in Sulfolobales and Methanothermobacter. In Thermococcales, a protein annotated as an Lhr2 protein was found in the network of proteins involved in RNA metabolism. To investigate this, we performed in-depth phylogenomic analyses to report the classification and taxonomic distribution of Lhr-type proteins in Archaea, and to better understand their relationship with bacterial Lhr. Furthermore, with the goal of envisioning the role(s) of aLhr2 in Thermococcales cells, we deciphered the enzymatic activities of aLhr2 from Thermococcus barophilus (Tbar). We showed that Tbar-aLhr2 is a DNA/RNA helicase with a significant annealing activity that is involved in processes dependent on DNA and RNA transactions.

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Genetic and Biochemical Characterizations of aLhr1 Helicase in the Thermophilic Crenarchaeon Sulfolobus acidocaldarius

et al. 2021

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Homologous recombination (HR) refers to the process of information exchange between homologous DNA duplexes and is composed of four main steps: end resection, strand invasion and formation of a Holliday junction (HJ), branch migration, and resolution of the HJ. Within each step of HR in Archaea, the helicase-promoting branch migration is not fully understood. Previous biochemical studies identified three candidates for archaeal helicase promoting branch migration in vitro: Hjm/Hel308, PINA, and archaeal long helicase related (aLhr) 2. However, there is no direct evidence of their involvement in HR in vivo. Here, we identified a novel helicase encoded by Saci_0814, isolated from the thermophilic crenarchaeon Sulfolobus acidocaldarius; the helicase dissociated a synthetic HJ. Notably, HR frequency in the Saci_0814-deleted strain was lower than that of the parent strain (5-fold decrease), indicating that Saci_0814 may be involved in HR in vivo. Saci_0814 is classified as an aLhr1 under superfamily 2 helicases; its homologs are conserved among Archaea. Purified protein produced in Escherichia coli showed branch migration activity in vitro. Based on both genetic and biochemical evidence, we suggest that aLhr1 is involved in HR and may function as a branch migration helicase in S. acidocaldarius.

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

Cited by 5 publications

References 45 publications

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

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

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

Genetic and Biochemical Characterizations of aLhr1 Helicase in the Thermophilic Crenarchaeon Sulfolobus acidocaldarius

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