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Relevant publications mentioning your query species (Methanosaeta concilii):

Relevant publications mentioning other organisms:

• Identification of essential and non-essential single-stranded DNA-binding proteins in a model archaeal organism.
  Skowyra A, MacNeill SA
  Nucleic Acids Res. 40(3):1077-90 (2012).

  
•  HVO_0291, HVO_1337   HVO_1336, Rpe, rpe  ...
• Abstract:
  Identification of essential and non-essential single-stranded DNA-binding proteins in a model archaeal organism Agnieszka Skowyra and Stuart A. MacNeill* School of Biology, University of St Andrews, North Haugh, St Andrews, Fife KY16 9TF, UK ABSTRACT Single-stranded DNA-binding proteins (SSBs) play vital roles in all aspects of DNA metabolism in all three domains of life and are characterized by the presence of one or more OB fold ssDNA-binding domains. Here, using the genetically tractable euryarchaeon Haloferax volcanii as a model, we present the first genetic analysis of SSB function in the archaea. We show that genes encoding the OB fold and zinc finger-containing RpaA1 and RpaB1 proteins are individually non-essential for cell viability but share an essential function, whereas the gene encoding the triple OB fold RpaC protein is essential. Loss of RpaC function can however be rescued by elevated expression of RpaB, indicative of functional overlap between the two classes of haloarchaeal SSB. Deletion analysis is used to demonstrate important roles for individual OB folds in RpaC and to show that conserved N- and C-terminal domains are required for efficient repair of DNA damage. Consistent with a role for RpaC in DNA repair, elevated expression of this protein leads to enhanced resistance to DNA damage. Taken together, our results offer important insights into archaeal SSB function and establish the haloarchaea as a valuable model for further studies. INTRODUCTION Single-stranded DNA-binding proteins (SSBs) are indispensable for many aspects of DNA metabolism including replication, repair and recombination, and play a vital role in the maintenance of genomic stability in all three domains of life (1,2). SSBs are characterized by the presence of one or more OB (oligosaccharide oligonucleotide binding) fold domains. OB folds consist of a ?ve-stranded b-sheet that is coiled to form a closed b-barrel, often capped by an a-helix (2,3). They range in length from 75 1...
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• Genetic and Biochemical Identification of a Novel Single-Stranded DNA-Binding Complex in Haloferax volcanii.
  Stroud A, Liddell S, Allers T
  Front Microbiol. 3:224 (2012).

  
•  RPA-associated protein, RPAP1, RPAP3, rpa-associated protein, rpap1, rpap3   rpe  ...
• Abstract:
  Amy Stroud 1, Susan Liddell 2 and Thorsten Allers 1 * School of Biology, Queen s Medical Centre, University of Nottingham, Nottingham, UK Division of Animal Sciences, University of Nottingham, Loughborough, UK Edited by: Zvi Kelman, University of Maryland, USA Reviewed by: Jocelyne DiRuggiero, The Johns Hopkins University, USA Stuart MacNeill, University of St Andrews, UK *Correspondence: Thorsten Allers, School of Biology, Queen s Medical Centre, University of Nottingham, Nottingham NG7 2UH, UK. e-mail: thorsten.allers@ nottingham.ac.uk Single-stranded DNA (ssDNA)-binding proteins play an essential role in DNA replication and repair. They use oligonucleotide/oligosaccharide-binding (OB)-folds, a ?ve-stranded ?-sheet coiled into a closed barrel, to bind to ssDNA thereby protecting and stabilizing the DNA. In eukaryotes the ssDNA-binding protein (SSB) is known as replication protein A (RPA) and consists of three distinct subunits that function as a heterotrimer. The bacterial homolog is termed SSB and functions as a homotetramer. In the archaeon Haloferax volcanii there are three genes encoding homologs of RPA. Two of the rpa genes (rpa1 and rpa3) exist in operons with a novel gene speci?c to Euryarchaeota; this gene encodes a protein that we have termed RPA-associated protein () (rpap). The rpap genes encode proteins belonging to COG3390 group and feature OB-folds, suggesting that they might cooperate with RPA in binding to ssDNA. Our genetic analysis showed that rpa1 and rpa3 deletion mutants have differing phenotypes; only ?rpa3 strains are hypersensitive to DNA damaging agents. Deletion of the rpa3-associated gene rpap3 () led to similar levels of DNA damage sensitivity, as did deletion of the rpa3 operon, suggesting that RPA3 and RPAP3 () function in the same pathway. Protein pull-downs involving recombinant hexahistidine-tagged RPAs showed that RPA3 co-puri?es with RPAP3 (), and RPA1 co-puri?es with RPAP1.This indicates that the RPAs interact only with their respective as...
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