Vaccinia Virus
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New enzyme research study findings have been reported from University of California
2009 JUL 20 - (NewsRx.com) -- According to a study from the United States, "Vaccinia virus protein VP55 translocates continuously with respect to single-stranded nucleic acid while extending its 3'end. Here, all key sites of polymerase-primer interaction were identified, demonstrating the wrapping or looping of polyadenylation primer around the polymerase during translocation." "Side-chain substitutions at one of the sites indicated its requirement for tail extension beyond similar to 12 nucleotides in length, and conformational changes observed upon oligonucleotide binding suggested allosteric connectivity during translocation. Conformational changes in VP39 upon VP55 binding suggested that, within the VP55-VP39 complex, VP39's mRNA 5' cap binding site closes," wrote C.Z. Li and colleagues, University of California. The researchers concluded: "The crystallographic structure showed a PAPase catalytic center without side-chain substitutions, possessing two metal ions and with all known reactive and catalytic groups represented, fitting a classical two-metal ion mechanism for phosphoryl transfer." Li and colleagues published the results of their research in Structure (Polymerase Translocation with Respect to Single-Stranded Nucleic Acid: Looping or Wrapping of Primer around a Poly(A) Polymerase. Structure, 2009;17(5):680-689). For additional information, contact P.D. Gershon, University of California, Dept. of Molecular Biology & Biochemistry, Irvine, CA 92697, USA. The publisher of the journal Structure can be contacted at: Cell Press, 600 Technology Square, 5TH Floor, Cambridge, MA 02139, USA. Keywords: United States, Irvine, Enzyme Research, Polymerase, University of California. This article was prepared by Proteomics Weekly editors from staff and other reports. Copyright 2009, Proteomics Weekly via NewsRx.com.
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