A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation

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dc.citation.firstpage3931en_US
dc.citation.issueNumber6en_US
dc.citation.journalTitleNucleic Acids Researchen_US
dc.citation.lastpage3942en_US
dc.citation.volumeNumber42en_US
dc.contributor.authorDesai, Kevin K.en_US
dc.contributor.authorCheng, Chin L.en_US
dc.contributor.authorBingman, Craig A.en_US
dc.contributor.authorPhillips, George N.Jr.en_US
dc.contributor.authorRaines, Ronald T.en_US
dc.date.accessioned2014-10-09T15:38:24Zen_US
dc.date.available2014-10-09T15:38:24Zen_US
dc.date.issued2014en_US
dc.description.abstractArchease is a 16-kDa protein that is conserved in all three domains of life. In diverse bacteria and archaea, the genes encoding Archease and the tRNA ligase RtcB are localized into an operon. Here we provide a rationale for this operon organization by showing that Archease and RtcB from Pyrococcus horikoshii function in tandem, with Archease altering the catalytic properties of the RNA ligase. RtcB catalyzes the GTP and Mn(II)-dependent joining of either 2′,3′-cyclic phosphate or 3′-phosphate termini to 5′-hydroxyl termini. We find that catalytic concentrations of Archease are sufficient to activate RtcB, and that Archease accelerates both the RNA 3′-P guanylylation and ligation steps. In addition, we show that Archease can alter the NTP specificity of RtcB such that ATP, dGTP or ITP is used efficiently. Moreover, RtcB variants that have inactivating substitutions in the guanine-binding pocket can be rescued by the addition of Archease. We also present a 1.4 Å-resolution crystal structure of P. horikoshii Archease that reveals a metal-binding site consisting of conserved carboxylates located at the protein tip. Substitution of the Archease metal-binding residues drastically reduced Archease-dependent activation of RtcB. Thus, evolution has sought to co-express archease and rtcB by creating a tRNA splicing operon.en_US
dc.identifier.citationDesai, Kevin K., Cheng, Chin L., Bingman, Craig A., et al.. "A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation." <i>Nucleic Acids Research,</i> 42, no. 6 (2014) Oxford University Press: 3931-3942. http://dx.doi.org/10.1093/nar/gkt1375.en_US
dc.identifier.doihttp://dx.doi.org/10.1093/nar/gkt1375en_US
dc.identifier.urihttps://hdl.handle.net/1911/77500en_US
dc.language.isoengen_US
dc.publisherOxford University Pressen_US
dc.rightsThis is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.en_US
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/en_US
dc.titleA tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligationen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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