News Column

Study Results from L. Xu and Colleagues Update Understanding of DNA-Directed RNA Polymerases (Dissecting the chemical interactions and substrate...

July 1, 2014



Study Results from L. Xu and Colleagues Update Understanding of DNA-Directed RNA Polymerases (Dissecting the chemical interactions and substrate structural signatures governing RNA polymerase II trigger loop closure by synthetic nucleic acid ...)

By a News Reporter-Staff News Editor at Life Science Weekly -- Investigators publish new report on Enzymes and Coenzymes. According to news reporting originating in Odense, Denmark, by NewsRx journalists, research stated, "The trigger loop (TL) of RNA polymerase II (Pol II) is a conserved structural motif that is crucial for Pol II catalytic activity and transcriptional fidelity. The TL remains in an inactive open conformation when the mismatched substrate is bound."

The news reporters obtained a quote from the research, "In contrast, TL switches from an inactive open state to a closed active state to facilitate nucleotide addition upon the binding of the cognate substrate to the Pol II active site. However, a comprehensive understanding of the specific chemical interactions and substrate structural signatures that are essential to this TL conformational change remains elusive. Here we employed synthetic nucleotide analogues as 'chemical mutation' tools coupling with alpha-amanitin transcription inhibition assay to systematically dissect the key chemical interactions and structural signatures governing the substrate-coupled TL closure in Saccharomyces cerevisiae Pol II. This study reveals novel insights into understanding the molecular basis of TL conformational transition upon substrate binding during Pol II transcription."

According to the news reporters, the research concluded: "This synthetic chemical biology approach may be extended to understand the mechanisms of other RNA polymerases as well as other nucleic acid enzymes in future studies."

For more information on this research see: Dissecting the chemical interactions and substrate structural signatures governing RNA polymerase II trigger loop closure by synthetic nucleic acid analogues. Nucleic Acids Research, 2014;42(9):5863-5870. Nucleic Acids Research can be contacted at: Oxford Univ Press, Great Clarendon St, Oxford OX2 6DP, England. (Oxford University Press - www.oup.com/; Nucleic Acids Research - nar.oxfordjournals.org)

Our news correspondents report that additional information may be obtained by contacting L. Xu, Univ Southern Denmark, Biomol Nanoscale Engn Center, Dept. of Phys Chem & Pharm, DK-5230 Odense M, Denmark. Additional authors for this research include K.V. Butler, J. Chong, J. Wengel, E.T. Kool and D. Wang (see also Enzymes and Coenzymes).

Keywords for this news article include: Odense, Europe, Denmark, RNA Polymerase II, Phosphotransferases, Enzymes and Coenzymes, Nucleotidyltransferases, DNA-Directed RNA Polymerases

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


For more stories covering the world of technology, please see HispanicBusiness' Tech Channel



Source: Life Science Weekly


Story Tools






HispanicBusiness.com Facebook Linkedin Twitter RSS Feed Email Alerts & Newsletters