The motor activity of DNA2 functions as an ssDNA translocase to promote DNA end resection
      
      
        
      
      
      
      
        
          
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Levikova, Maryna
  Institute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland
          
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Pinto, Cosimo
  Institute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland
          
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Cejka, Petr
  Institute of Molecular Cancer Research, University of Zurich, 8057 Zurich, Switzerland - Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
          
 
      
      
      
      
      
      
      
      
      
      
      
      
      
      
      
        
        Published in:
        
          
            
            - Genes and Development. - Cold Spring Harbor Laboratory Press. - 2017, vol. 31, no. 5, p. 493-502
 
       
      
      
      
      
      
       
      
      
      
        
        English
        
        
        
          DNA2 nuclease–helicase functions in DNA replication and recombination. This requires the nuclease of DNA2, while, in  contrast, the role of the helicase activity has been unclear. We now show that the motor activity of both recombinant  yeast and human DNA2 promotes efficient degradation of long stretches of ssDNA, particularly in the presence of the  replication protein A. This degradation is further stimulated by a direct interaction with a cognate RecQ family helicase,  which functions with DNA2 in DNA end resection to initiate homologous recombination. Consequently, helicase- deficient yeast dna2 K1080E cells display reduced resection speed of HO-induced DNA double-strand breaks. These  results support a model of DNA2 and the RecQ family helicase partner forming a bidirectional motor machine, where  the RecQ family helicase is the lead helicase, and the motor of DNA2 functions as a ssDNA translocase to promote  degradation of 5'-terminated DNA.
        
        
       
      
      
      
        
        
        
        
        
        
        
        
        
        
        
        
        
        
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                  Biological sciences
                
              
            
          
        
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          Open access status
        
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          hybrid
        
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  RERO DOC
  
    
      324121
    
  
            
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      ark:/12658/srd1318829
    
  
            
 
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          https://n2t.net/ark:/12658/srd1318829
        
 
   
  
  
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