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  • Translocation-coupled DNA cleavage by the Type ISP restriction-modification enzymes 
    Chand, Mahesh K; NIRWAN, NEHA; Diffin, Fiona M; Aelst, Kara van; Kulkarni, Manasi; Pernstich, Christian; Szczelkun, Mark D; KAYARAT, SAIKRISHNAN (Nature Publishing Group, 2015-09)
    Production of endonucleolytic double-strand DNA breaks requires separate strand cleavage events. Although catalytic mechanisms for simple, dimeric endonucleases are known, there are many complex nuclease machines that are ...
  • Structural insights into DNA sequence recognition by Type ISP restriction-modification enzymes 
    Kulkarni, Manasi; NIRWAN, NEHA; Aelst, Kara van; Szczelkun, Mark D; KAYARAT, SAIKRISHNAN (Oxford University Press, 2016-03)
    Engineering restriction enzymes with new sequence specificity has been an unaccomplished challenge, presumably because of the complexity of target recognition. Here we report detailed analyses of target recognition by Type ...
  • Hexameric assembly of the AAA+ protein McrB is necessary for GTPase activity 
    NIRWAN, NEHA; SINGH, PRATIMA; MISHRA, GYANA GOURAB; Johnson, Christopher M; Szczelkun, Mark D; Inoue, Katsuaki; Vinothkumar, Kutti R.; KAYARAT, SAIKRISHNAN (Oxford University Press, 2019-01)
    McrBC is one of the three modification-dependent restriction enzymes encoded by the Escherichia coli K12 chromosome. Amongst restriction enzymes, McrBC and its close homologues are unique in employing the AAA+ domain for ...
  • Structure-based mechanism for activation of the AAA+ GTPase McrB by the endonuclease McrC 
    NIRWAN, NEHA; Itoh, Yuzuru; SINGH, PRATIMA; BANDYOPADHYAY, SUTIRTHA; Vinothkumar, Kutti R.; Amunts, Alexey; KAYARAT, SAIKRISHNAN (Nature Publishing Group, 2019-07)
    The AAA+ GTPase McrB powers DNA cleavage by the endonuclease McrC. The GTPase itself is activated by McrC. The architecture of the GTPase and nuclease complex, and the mechanism of their activation remained unknown. Here, ...

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