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Studies in the area of cell biology reported from K. Saikrishnan and co-researchers
2009 AUG 4 - (NewsRx.com) -- "Superfamily 1B (SF1B) helicases translocate in a 5'-3' direction and are required for a range of cellular activities across all domains of life. However, structural analyses to date have focused on how SF1A helicases achieve 3'-5' movement along nucleic acids," scientists in Potters Bar, the United Kingdom report. "We present crystal structures of the complex between the SF1B helicase RecD2 from Deinococcus radiodurans and ssDNA in the presence and absence of an ATP analog. These snapshots of the reaction pathway reveal a nucleotide binding-induced conformational change of the two motor domains that is broadly reminiscent of changes observed in other SF1 and SF2 helicases. Together with biochemical data, the structures point to a step size for translocation of one base per ATP hydrolyzed," wrote K. Saikrishnan and colleagues. The researchers concluded: "Moreover, the structures also reveal a mechanism for nucleic acid translocation in the 5'-3' direction by SF1B helicases that is surprisingly different from that of 3'-5' translocation by SF1A enzymes, and explains the molecular basis of directionality.." Saikrishnan and colleagues published their study in Cell (Mechanistic Basis of 5'-3' Translocation in SF1B Helicases. Cell, 2009;137(5):849-859). For additional information, contact D.B. Wigley, London Research Institute, Clare Hall Laboratories, Cancer Research UK, Blanche Lane, Potters Bar EN6 3LD, Herts, UK. The publisher's contact information for the journal Cell is: Cell Press, 600 Technology Square, 5TH Floor, Cambridge, MA 02139, USA. Keywords: United Kingdom, Potters Bar, Life Sciences, Enzyme Research, Helicase, Cell Biology. This article was prepared by Science Letter editors from staff and other reports. Copyright 2009, Science Letter via NewsRx.com.
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