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Lookup NU author(s): Dr Yulia Yuzenkova, Professor Nikolay ZenkinORCiD
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The active center of RNA polymerase can hydrolyze phosphodiester bonds in nascent RNA, a reaction thought to be important for proofreading of transcription. The reaction proceeds via a general two Mg2+ mechanism and is assisted by the 3' end nucleotide of the transcript. Here, by using Thermus aquaticus RNA polymerase, we show that the reaction also requires the flexible domain of the active center, the trigger loop (TL). We show that the invariant histidine (beta' His1242) of the TL is essential for hydrolysis/proof-reading and participates in the reaction in two distinct ways: by positioning the 3' end nucleotide of the transcript that assists catalysis and/or by directly participating in the reaction as a general base. We also show that participation of the beta' His1242 of the TL in phosphodiester bond hydrolysis does not depend on the extent of elongation complex backtracking. We obtained similar results with Escherichia coli RNA polymerase, indicating that the function of the TL in phosphodiester bond hydrolysis is conserved among bacteria.
Author(s): Yuzenkova Y, Zenkin N
Publication type: Article
Publication status: Published
Journal: Proceedings of the National Academy of Sciences
Year: 2010
Volume: 107
Issue: 24
Pages: 10878-10883
Print publication date: 01/06/2010
ISSN (print): 0027-8424
ISSN (electronic): 1091-6490
Publisher: National Academy of Sciences
URL: http://dx.doi.org/10.1073/pnas.0914424107
DOI: 10.1073/pnas.0914424107
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