The Mrs1 splicing factor binds the bI3 group I intron at each of two tetraloop-receptor motifs.

PloS One
Caia D S Duncan, K M Weeks

Abstract

Most large ribozymes require protein cofactors in order to function efficiently. The yeast mitochondrial bI3 group I intron requires two proteins for efficient splicing, Mrs1 and the bI3 maturase. Mrs1 has evolved from DNA junction resolvases to function as an RNA cofactor for at least two group I introns; however, the RNA binding site and the mechanism by which Mrs1 facilitates splicing were unknown. Here we use high-throughput RNA structure analysis to show that Mrs1 binds a ubiquitous RNA tertiary structure motif, the GNRA tetraloop-receptor interaction, at two sites in the bI3 RNA. Mrs1 also interacts at similar tetraloop-receptor elements, as well as other structures, in the self-folding Azoarcus group I intron and in the RNase P enzyme. Thus, Mrs1 recognizes general features found in the tetraloop-receptor motif. Identification of the two Mrs1 binding sites now makes it possible to create a model of the complete six-component bI3 ribonucleoprotein. All protein cofactors bind at the periphery of the RNA such that every long-range RNA tertiary interaction is stabilized by protein binding, involving either Mrs1 or the bI3 maturase. This work emphasizes the strong evolutionary pressure to bolster RNA tertiary structure with R...Continue Reading

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Citations

May 28, 2011·Accounts of Chemical Research·Kevin M Weeks, David M Mauger
Apr 17, 2012·Nature Methods·Feng DingNikolay V Dokholyan
Jun 7, 2013·Mobile DNA·Annica Hedberg, Steinar D Johansen
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Sep 22, 2017·Nucleic Acids Research·Saikat Chakraborty, Yamuna Krishnan
Dec 11, 2013·Physical Chemistry Chemical Physics : PCCP·Zhaojian HeShi-Jie Chen
Nov 7, 2019·Yeast·Bernard Dujon

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Methods Mentioned

BETA
footprinting
PCR
electrophoresis

Software Mentioned

TASSER
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lsqman
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