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dc.contributor.authorDesai, Kevin K.
Cheng, Chin L.
Bingman, Craig A.
Phillips, George N. Jr.
Raines, Ronald T.
dc.date.accessioned 2014-10-09T15:38:24Z
dc.date.available 2014-10-09T15:38:24Z
dc.date.issued 2014
dc.identifier.citation Desai, 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." Nucleic Acids Research, 42, no. 6 (2014) Oxford University Press: 3931-3942. http://dx.doi.org/10.1093/nar/gkt1375.
dc.identifier.urihttps://hdl.handle.net/1911/77500
dc.description.abstract Archease 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.
dc.language.iso eng
dc.publisher Oxford University Press
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.
dc.rights.urihttps://creativecommons.org/licenses/by/3.0/
dc.title A tRNA splicing operon: Archease endows RtcB with dual GTP/ATP cofactor specificity and accelerates RNA ligation
dc.type Journal article
dc.contributor.funder National Institutes of Health
dc.contributor.funder National Cancer Institute/National Institute of General Medical Sciences
dc.contributor.funder U.S. Department of Energy, Basic Energy Sciences, Office of Science
dc.citation.journalTitle Nucleic Acids Research
dc.citation.volumeNumber 42
dc.citation.issueNumber 6
dc.type.dcmi Text
dc.identifier.doihttp://dx.doi.org/10.1093/nar/gkt1375
dc.identifier.pmcid PMC3973293
dc.identifier.pmid 24435797
dc.identifier.grantID F32GM100681 (National Institutes of Health)
dc.identifier.grantID U01GM098248 (National Institutes of Health)
dc.identifier.grantID U54GM074901 (National Institutes of Health)
dc.identifier.grantID R01CA073808 (National Institutes of Health)
dc.identifier.grantID Y1-CO-1020 (National Cancer Institute/National Institute of General Medical Sciences)
dc.identifier.grantID Y1-GM-1104 (National Cancer Institute/National Institute of General Medical Sciences)
dc.identifier.grantID DE-AC02-06CH11357 (U.S. Department of Energy, Basic Energy Sciences, Office of Science)
dc.identifier.grantID R01CA073808 (National Institutes of Health)
dc.type.publication publisher version
dc.citation.firstpage 3931
dc.citation.lastpage 3942


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This 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.
Except where otherwise noted, this item's license is described as This 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.