All Outputs (2)

Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae. (2002)
Journal Article
Ingleston, S., Dickman, M., Grasby, J., Hornby, D., Sharples, G., & Lloyd, R. (2002). Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae. European journal of biochemistry (Internet), 269, 1525-1533

The RuvA, RuvB and RuvC proteins of Escherichia coli act together to process Holliday junctions formed during recombination and DNA repair. RuvA has a well-defined DNA binding surface that is sculptured specifically to accommodate a Holliday junction... Read More about Holliday junction binding and processing by the RuvA protein of Mycoplasma pneumoniae..

RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions (2002)
Journal Article
Sharples, G., Bolt, E., & Lloyd, R. (2002). RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions. Molecular Microbiology, 44(2), 549-559. https://doi.org/10.1046/j.1365-2958.2002.02916.x

The RusA protein of Escherichia coli is a DNA structure-specific endonuclease that resolves Holliday junction intermediates formed during DNA replication, recombination and repair by introducing symmetrically paired incisions 5' to CC dinucleotides.... Read More about RusA proteins from the extreme thermophile Aquifex aeolicus and lactococcal phage r1t resolve Holliday junctions.