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Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10

Pseudouridines (Ψ) are found in structurally and functionally important regions of RNAs. Six families of Ψ synthases, TruA, TruB, TruD, RsuA, RluA, and Pus10 have been identified. Pus10 is present in Archaea and Eukarya. While most archaeal Pus10 produce both tRNA Ψ54 and Ψ55, some produce only Ψ55....

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Autores principales: Joardar, Archi, Jana, Sujata, Fitzek, Elisabeth, Gurha, Priyatansh, Majumder, Mrinmoyee, Chatterjee, Kunal, Geisler, Matt, Gupta, Ramesh
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753934/
https://www.ncbi.nlm.nih.gov/pubmed/23898217
http://dx.doi.org/10.1261/rna.039230.113
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author Joardar, Archi
Jana, Sujata
Fitzek, Elisabeth
Gurha, Priyatansh
Majumder, Mrinmoyee
Chatterjee, Kunal
Geisler, Matt
Gupta, Ramesh
author_facet Joardar, Archi
Jana, Sujata
Fitzek, Elisabeth
Gurha, Priyatansh
Majumder, Mrinmoyee
Chatterjee, Kunal
Geisler, Matt
Gupta, Ramesh
author_sort Joardar, Archi
collection PubMed
description Pseudouridines (Ψ) are found in structurally and functionally important regions of RNAs. Six families of Ψ synthases, TruA, TruB, TruD, RsuA, RluA, and Pus10 have been identified. Pus10 is present in Archaea and Eukarya. While most archaeal Pus10 produce both tRNA Ψ54 and Ψ55, some produce only Ψ55. Interestingly, human PUS10 has been implicated in apoptosis and Crohn’s and Celiac diseases. Homology models of archaeal Pus10 proteins based on the crystal structure of human PUS10 reveal that there are subtle structural differences in all of these Pus10 proteins. These observations suggest that structural changes in homologous proteins may lead to loss, gain, or change of their functions, warranting the need to study the structure-function relationship of these proteins. Using comparison of structural models and a series of mutations, we identified forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its Ψ54, but not for its Ψ55 activity. We also found that a Leu residue, in addition to the catalytic Asp, is essential for both activities. Since forefinger loop is needed for both rRNA and tRNA Ψ synthase activities of RluA, but only for tRNA Ψ54 activity of Pus10, archaeal Pus10 proteins must use a different mechanism of recognition for Ψ55 activity. We propose that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. However, since we did not observe any mutation that affected only Ψ55 activity, both mechanisms for archaeal Pus10 activities must share some common features.
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spelling pubmed-37539342014-09-01 Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10 Joardar, Archi Jana, Sujata Fitzek, Elisabeth Gurha, Priyatansh Majumder, Mrinmoyee Chatterjee, Kunal Geisler, Matt Gupta, Ramesh RNA Articles Pseudouridines (Ψ) are found in structurally and functionally important regions of RNAs. Six families of Ψ synthases, TruA, TruB, TruD, RsuA, RluA, and Pus10 have been identified. Pus10 is present in Archaea and Eukarya. While most archaeal Pus10 produce both tRNA Ψ54 and Ψ55, some produce only Ψ55. Interestingly, human PUS10 has been implicated in apoptosis and Crohn’s and Celiac diseases. Homology models of archaeal Pus10 proteins based on the crystal structure of human PUS10 reveal that there are subtle structural differences in all of these Pus10 proteins. These observations suggest that structural changes in homologous proteins may lead to loss, gain, or change of their functions, warranting the need to study the structure-function relationship of these proteins. Using comparison of structural models and a series of mutations, we identified forefinger loop (reminiscent of that of RluA) and an Arg and a Tyr residue of archaeal Pus10 as critical determinants for its Ψ54, but not for its Ψ55 activity. We also found that a Leu residue, in addition to the catalytic Asp, is essential for both activities. Since forefinger loop is needed for both rRNA and tRNA Ψ synthase activities of RluA, but only for tRNA Ψ54 activity of Pus10, archaeal Pus10 proteins must use a different mechanism of recognition for Ψ55 activity. We propose that archaeal Pus10 uses two distinct mechanisms for substrate uridine recognition and binding. However, since we did not observe any mutation that affected only Ψ55 activity, both mechanisms for archaeal Pus10 activities must share some common features. Cold Spring Harbor Laboratory Press 2013-09 /pmc/articles/PMC3753934/ /pubmed/23898217 http://dx.doi.org/10.1261/rna.039230.113 Text en © 2013; Published by Cold Spring Harbor Laboratory Press for the RNA Society http://creativecommons.org/licenses/by-nc/3.0/ This article is distributed exclusively by the RNA Society for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 3.0 Unported), as described at http://creativecommons.org/licenses/by-nc/3.0/.
spellingShingle Articles
Joardar, Archi
Jana, Sujata
Fitzek, Elisabeth
Gurha, Priyatansh
Majumder, Mrinmoyee
Chatterjee, Kunal
Geisler, Matt
Gupta, Ramesh
Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title_full Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title_fullStr Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title_full_unstemmed Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title_short Role of forefinger and thumb loops in production of Ψ54 and Ψ55 in tRNAs by archaeal Pus10
title_sort role of forefinger and thumb loops in production of ψ54 and ψ55 in trnas by archaeal pus10
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3753934/
https://www.ncbi.nlm.nih.gov/pubmed/23898217
http://dx.doi.org/10.1261/rna.039230.113
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