1. Finding the right match fast.

    Cell 160(5):809 (2015) PMID 25723158

    DNA recombinases face the daunting task of locating and pairing up specific sequences among millions of base pairs in a genome, all within about an hour. Qi et al. show that recombinases solve this problem by searching in 8-nt microhomology units, reducing the search space and accelerating the h...
  2. Finding the right match fast.

    Cell 160(5):809 (2015) PMID 25723158

    DNA recombinases face the daunting task of locating and pairing up specific sequences among millions of base pairs in a genome, all within about an hour. Qi et al. show that recombinases solve this problem by searching in 8-nt microhomology units, reducing the search space and accelerating the h...
  3. Finding the Right Match Fast

    Cell 160(5):809 (2015)

    DNA recombinases face the daunting task of locating and pairing up specific sequences among millions of base pairs in a genome, all within about an hour. Qi et al. show that recombinases solve this problem by searching in 8-nt microhomology units, reducing the search space and accelera...
  4. Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.

    eLife 4 (2015) PMID 25970034 PMCID PMC4460406

    Leading strand DNA synthesis requires functional coupling between replicative helicase and DNA polymerase (DNAP) enzymes, but the structural and mechanistic basis of coupling is poorly understood. This study defines the precise positions of T7 helicase and T7 DNAP at the replication fork junctio...
  5. Relaxed rotational and scrunching changes in P266L mutant of T7 RNA polymerase reduce short abortive RNAs while delaying transition into elongation.

    PLoS ONE 9(3):e91859 (2014) PMID 24651161 PMCID PMC3961267

    Abortive cycling is a universal feature of transcription initiation catalyzed by DNA-dependent RNA polymerases (RNAP). In bacteriophage T7 RNAP, mutation of proline 266 to leucine (P266L) in the C-linker region connecting the N-terminal promoter binding domain with the C-terminal catalytic domai...
  6. Relaxed rotational and scrunching changes in P266L mutant of T7 RNA polymerase reduce short abortive RNAs while delaying transition into elongation.

    PLoS ONE 9(3):e91859 (2014) PMID 24651161 PMCID PMC3961267

    Abortive cycling is a universal feature of transcription initiation catalyzed by DNA-dependent RNA polymerases (RNAP). In bacteriophage T7 RNAP, mutation of proline 266 to leucine (P266L) in the C-linker region connecting the N-terminal promoter binding domain with the C-terminal catalytic domai...
  7. Relaxed rotational and scrunching changes in P266L mutant of T7 RNA polymerase reduce short abortive RNAs while delaying transition into elongation.

    PLoS ONE 9(3):e91859 (2014) PMID 24651161 PMCID PMC3961267

    Abortive cycling is a universal feature of transcription initiation catalyzed by DNA-dependent RNA polymerases (RNAP). In bacteriophage T7 RNAP, mutation of proline 266 to leucine (P266L) in the C-linker region connecting the N-terminal promoter binding domain with the C-terminal catalytic domai...
  8. Human mitochondrial DNA helicase TWINKLE is both an unwinding and annealing helicase.

    Journal of Biological Chemistry 287(18):14545 (2012) PMID 22383523 PMCID PMC3340288

    TWINKLE is a nucleus-encoded human mitochondrial (mt)DNA helicase. Point mutations in TWINKLE are associated with heritable neuromuscular diseases characterized by deletions in the mtDNA. To understand the biochemical basis of these diseases, it is important to define the roles of TWINKLE in mtD...
  9. Human mitochondrial DNA helicase TWINKLE is both an unwinding and annealing helicase.

    Journal of Biological Chemistry 287(18):14545 (2012) PMID 22383523 PMCID PMC3340288

    TWINKLE is a nucleus-encoded human mitochondrial (mt)DNA helicase. Point mutations in TWINKLE are associated with heritable neuromuscular diseases characterized by deletions in the mtDNA. To understand the biochemical basis of these diseases, it is important to define the roles of TWINKLE in mtD...
  10. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase.

    Current Opinion in Chemical Biology 15(5):595 (2011) PMID 21865075 PMCID PMC3189298

    Helicases are molecular motor proteins that couple NTP hydrolysis to directional movement along nucleic acids. A class of helicases characterized by their ring-shaped hexameric structures translocate processively and unidirectionally along single-stranded (ss) DNA to separate the strands of doub...
  11. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase.

    Current Opinion in Chemical Biology 15(5):595 (2011) PMID 21865075 PMCID PMC3189298

    Helicases are molecular motor proteins that couple NTP hydrolysis to directional movement along nucleic acids. A class of helicases characterized by their ring-shaped hexameric structures translocate processively and unidirectionally along single-stranded (ss) DNA to separate the strands of doub...
  12. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase.

    Current Opinion in Chemical Biology 15(5):595 (2011) PMID 21865075 PMCID PMC3189298

    Helicases are molecular motor proteins that couple NTP hydrolysis to directional movement along nucleic acids. A class of helicases characterized by their ring-shaped hexameric structures translocate processively and unidirectionally along single-stranded (ss) DNA to separate the strands of doub...
  13. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase

    Current Opinion in Chemical Biology 15(5):595 (2011)

    Highlights ► Recent nucleic acid bound structures of hexameric helicases reveal mechanism and polarity of translocation along ssDNA. ► Hexameric helicases unwind dsDNA by an active or a passive mechanism. ► Replicative helicases mediate physical and functional coupling with the DNA pol...
  14. Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase

    Current Opinion in Chemical Biology 15(5):595 (2011) PMID 21865075 PMCID PMC3189298

    Highlights ► Recent nucleic acid bound structures of hexameric helicases reveal mechanism and polarity of translocation along ssDNA. ► Hexameric helicases unwind dsDNA by an active or a passive mechanism. ► Replicative helicases mediate physical and functional coupling with the DNA pol...