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RNase MRP and the RNA processing cascade in the eukaryotic ancestor

BACKGROUND: Within eukaryotes there is a complex cascade of RNA-based macromolecules that process other RNA molecules, especially mRNA, tRNA and rRNA. An example is RNase MRP processing ribosomal RNA (rRNA) in ribosome biogenesis. One hypothesis is that this complexity was present early in eukaryoti...

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Autores principales: Woodhams, Michael D, Stadler, Peter F, Penny, David, Collins, Lesley J
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1796607/
https://www.ncbi.nlm.nih.gov/pubmed/17288571
http://dx.doi.org/10.1186/1471-2148-7-S1-S13
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author Woodhams, Michael D
Stadler, Peter F
Penny, David
Collins, Lesley J
author_facet Woodhams, Michael D
Stadler, Peter F
Penny, David
Collins, Lesley J
author_sort Woodhams, Michael D
collection PubMed
description BACKGROUND: Within eukaryotes there is a complex cascade of RNA-based macromolecules that process other RNA molecules, especially mRNA, tRNA and rRNA. An example is RNase MRP processing ribosomal RNA (rRNA) in ribosome biogenesis. One hypothesis is that this complexity was present early in eukaryotic evolution; an alternative is that an initial simpler network later gained complexity by gene duplication in lineages that led to animals, fungi and plants. Recently there has been a rapid increase in support for the complexity-early theory because the vast majority of these RNA-processing reactions are found throughout eukaryotes, and thus were likely to be present in the last common ancestor of living eukaryotes, herein called the Eukaryotic Ancestor. RESULTS: We present an overview of the RNA processing cascade in the Eukaryotic Ancestor and investigate in particular, RNase MRP which was previously thought to have evolved later in eukaryotes due to its apparent limited distribution in fungi and animals and plants. Recent publications, as well as our own genomic searches, find previously unknown RNase MRP RNAs, indicating that RNase MRP has a wide distribution in eukaryotes. Combining secondary structure and promoter region analysis of RNAs for RNase MRP, along with analysis of the target substrate (rRNA), allows us to discuss this distribution in the light of eukaryotic evolution. CONCLUSION: We conclude that RNase MRP can now be placed in the RNA-processing cascade of the Eukaryotic Ancestor, highlighting the complexity of RNA-processing in early eukaryotes. Promoter analyses of MRP-RNA suggest that regulation of the critical processes of rRNA cleavage can vary, showing that even these key cellular processes (for which we expect high conservation) show some species-specific variability. We present our consensus MRP-RNA secondary structure as a useful model for further searches.
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spelling pubmed-17966072007-02-09 RNase MRP and the RNA processing cascade in the eukaryotic ancestor Woodhams, Michael D Stadler, Peter F Penny, David Collins, Lesley J BMC Evol Biol Research BACKGROUND: Within eukaryotes there is a complex cascade of RNA-based macromolecules that process other RNA molecules, especially mRNA, tRNA and rRNA. An example is RNase MRP processing ribosomal RNA (rRNA) in ribosome biogenesis. One hypothesis is that this complexity was present early in eukaryotic evolution; an alternative is that an initial simpler network later gained complexity by gene duplication in lineages that led to animals, fungi and plants. Recently there has been a rapid increase in support for the complexity-early theory because the vast majority of these RNA-processing reactions are found throughout eukaryotes, and thus were likely to be present in the last common ancestor of living eukaryotes, herein called the Eukaryotic Ancestor. RESULTS: We present an overview of the RNA processing cascade in the Eukaryotic Ancestor and investigate in particular, RNase MRP which was previously thought to have evolved later in eukaryotes due to its apparent limited distribution in fungi and animals and plants. Recent publications, as well as our own genomic searches, find previously unknown RNase MRP RNAs, indicating that RNase MRP has a wide distribution in eukaryotes. Combining secondary structure and promoter region analysis of RNAs for RNase MRP, along with analysis of the target substrate (rRNA), allows us to discuss this distribution in the light of eukaryotic evolution. CONCLUSION: We conclude that RNase MRP can now be placed in the RNA-processing cascade of the Eukaryotic Ancestor, highlighting the complexity of RNA-processing in early eukaryotes. Promoter analyses of MRP-RNA suggest that regulation of the critical processes of rRNA cleavage can vary, showing that even these key cellular processes (for which we expect high conservation) show some species-specific variability. We present our consensus MRP-RNA secondary structure as a useful model for further searches. BioMed Central 2007-02-08 /pmc/articles/PMC1796607/ /pubmed/17288571 http://dx.doi.org/10.1186/1471-2148-7-S1-S13 Text en Copyright © 2007 Woodhams et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Woodhams, Michael D
Stadler, Peter F
Penny, David
Collins, Lesley J
RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title_full RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title_fullStr RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title_full_unstemmed RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title_short RNase MRP and the RNA processing cascade in the eukaryotic ancestor
title_sort rnase mrp and the rna processing cascade in the eukaryotic ancestor
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1796607/
https://www.ncbi.nlm.nih.gov/pubmed/17288571
http://dx.doi.org/10.1186/1471-2148-7-S1-S13
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