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Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z

tRNase Z, a member of the metallo-β-lactamase family, endonucleolytically removes the pre-tRNA 3′ trailer in a step central to tRNA maturation. The short form (tRNase Z(S)) is the only one found in bacteria and archaebacteria and is also present in some eukaryotes. The homologous long form (tRNase Z...

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Autores principales: Wilson, Christopher, Ramai, Daryl, Serjanov, Dmitri, Lama, Neema, Levinger, Louis, Chang, Emmanuel J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3714273/
https://www.ncbi.nlm.nih.gov/pubmed/23874404
http://dx.doi.org/10.1371/journal.pone.0066942
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author Wilson, Christopher
Ramai, Daryl
Serjanov, Dmitri
Lama, Neema
Levinger, Louis
Chang, Emmanuel J.
author_facet Wilson, Christopher
Ramai, Daryl
Serjanov, Dmitri
Lama, Neema
Levinger, Louis
Chang, Emmanuel J.
author_sort Wilson, Christopher
collection PubMed
description tRNase Z, a member of the metallo-β-lactamase family, endonucleolytically removes the pre-tRNA 3′ trailer in a step central to tRNA maturation. The short form (tRNase Z(S)) is the only one found in bacteria and archaebacteria and is also present in some eukaryotes. The homologous long form (tRNase Z(L)), exclusively found in eukaryotes, consists of related amino- and carboxy-domains, suggesting that tRNase Z(L) arose from a tandem duplication of tRNase Z(S) followed by interdependent divergence of the domains. X-ray crystallographic structures of tRNase Z(S) reveal a flexible arm (FA) extruded from the body of tRNase Z remote from the active site that binds tRNA far from the scissile bond. No tRNase Z(L) structures have been solved; alternative biophysical studies are therefore needed to illuminate its functional characteristics. Structural analyses of tRNase Z(L) performed by limited proteolysis, two dimensional gel electrophoresis and mass spectrometry establish stability of the amino and carboxy domains and flexibility of the FA and inter-domain tether, with implications for tRNase Z(L) function.
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spelling pubmed-37142732013-07-19 Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z Wilson, Christopher Ramai, Daryl Serjanov, Dmitri Lama, Neema Levinger, Louis Chang, Emmanuel J. PLoS One Research Article tRNase Z, a member of the metallo-β-lactamase family, endonucleolytically removes the pre-tRNA 3′ trailer in a step central to tRNA maturation. The short form (tRNase Z(S)) is the only one found in bacteria and archaebacteria and is also present in some eukaryotes. The homologous long form (tRNase Z(L)), exclusively found in eukaryotes, consists of related amino- and carboxy-domains, suggesting that tRNase Z(L) arose from a tandem duplication of tRNase Z(S) followed by interdependent divergence of the domains. X-ray crystallographic structures of tRNase Z(S) reveal a flexible arm (FA) extruded from the body of tRNase Z remote from the active site that binds tRNA far from the scissile bond. No tRNase Z(L) structures have been solved; alternative biophysical studies are therefore needed to illuminate its functional characteristics. Structural analyses of tRNase Z(L) performed by limited proteolysis, two dimensional gel electrophoresis and mass spectrometry establish stability of the amino and carboxy domains and flexibility of the FA and inter-domain tether, with implications for tRNase Z(L) function. Public Library of Science 2013-07-17 /pmc/articles/PMC3714273/ /pubmed/23874404 http://dx.doi.org/10.1371/journal.pone.0066942 Text en © 2013 Wilson et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Wilson, Christopher
Ramai, Daryl
Serjanov, Dmitri
Lama, Neema
Levinger, Louis
Chang, Emmanuel J.
Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title_full Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title_fullStr Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title_full_unstemmed Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title_short Tethered Domains and Flexible Regions in tRNase Z(L), the Long Form of tRNase Z
title_sort tethered domains and flexible regions in trnase z(l), the long form of trnase z
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3714273/
https://www.ncbi.nlm.nih.gov/pubmed/23874404
http://dx.doi.org/10.1371/journal.pone.0066942
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