News Column

New Data from Boston University School of Medicine Illuminate Findings in Viral RNA (Surface for catalysis by poliovirus RNA-dependent RNA polymerase)

July 1, 2014

By a News Reporter-Staff News Editor at Life Science Weekly -- Current study results on Viral RNA have been published. According to news reporting out of Boston, Massachusetts, by NewsRx editors, research stated, "The poliovirus RNA-dependent RNA polymerase, 3Dpol, replicates the viral genomic RNA on the surface of virus-induced intracellular membranes. Macromolecular assemblies of 3Dpol form linear arrays of subunits that propagate along a strong protein-protein interaction called interface-I, as was observed in the crystal structure of wild-type poliovirus polymerase."

Our news journalists obtained a quote from the research from the Boston University School of Medicine, "These 'filaments' recur with slight modifications in planar sheets and, with additional modifications that accommodate curvature, in helical tubes of the polymerase, by packing filaments together via a second set of interactions. Periodic variations of subunit orientations within 3Dpol tubes give rise to 'ghost reflections' in diffraction patterns computed from electron cryomicrographs of helical arrays. The ghost reflections reveal that polymerase tubes are formed by bundles of four to five interface-I filaments, which are then connected to the next bundle of filaments with a perturbation of interface interactions between bundles. While enzymatically inactive polymerase is also capable of oligomerization, much thinner tubes that lack interface-I interactions between adjacent subunits are formed, suggesting that long-range allostery produces conformational changes that extend from the active site to the protein-protein interface. Macromolecular assemblies of poliovirus polymerase show repeated use of flexible interface interactions for polymerase lattice formation, suggesting that adaptability of polymerase-polymerase interactions facilitates RNA replication."

According to the news editors, the research concluded: "In addition, the presence of a positively charged groove identified in polymerase arrays may help position and stabilize the RNA template during replication."

For more information on this research see: Surface for catalysis by poliovirus RNA-dependent RNA polymerase. Jmb Online, 2013;425(14):2529-40 (see also Viral RNA).

Our news journalists report that additional information may be obtained by contacting J. Wang, Dept. of Physiology and Biophysics, Boston University School of Medicine, 700 Albany Street, Boston, MA 02118, United States. Additional authors for this research include J.M. Lyle and E. Bullitt.

Keywords for this news article include: Boston, Viral RNA, Polymerase, Massachusetts, United States, Nanotechnology, Emerging Technologies, Enzymes and Coenzymes, North and Central America, Macromolecular Assemblies.

Our reports deliver fact-based news of research and discoveries from around the world. Copyright 2014, NewsRx LLC

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Source: Life Science Weekly

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