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The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development
Methylation of nucleotides in ribosomal RNAs (rRNAs) is a ubiquitous feature that occurs in all living organisms. The formation of methylated nucleotides is performed by a variety of RNA-methyltransferases. Chloroplasts of plant cells result from an endosymbiotic event and possess their own genome a...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Oxford University Press
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102989/ https://www.ncbi.nlm.nih.gov/pubmed/32095829 http://dx.doi.org/10.1093/nar/gkaa129 |
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author | Zou, Meijuan Mu, Ying Chai, Xin Ouyang, Min Yu, Long-Jiang Zhang, Lixin Meurer, Jörg Chi, Wei |
author_facet | Zou, Meijuan Mu, Ying Chai, Xin Ouyang, Min Yu, Long-Jiang Zhang, Lixin Meurer, Jörg Chi, Wei |
author_sort | Zou, Meijuan |
collection | PubMed |
description | Methylation of nucleotides in ribosomal RNAs (rRNAs) is a ubiquitous feature that occurs in all living organisms. The formation of methylated nucleotides is performed by a variety of RNA-methyltransferases. Chloroplasts of plant cells result from an endosymbiotic event and possess their own genome and ribosomes. However, enzymes responsible for rRNA methylation and the function of modified nucleotides in chloroplasts remain to be determined. Here, we identified an rRNA methyltransferase, CMAL (Chloroplast MraW-Like), in the Arabidopsis chloroplast and investigated its function. CMAL is the Arabidopsis ortholog of bacterial MraW/ RsmH proteins and accounts to the N(4)-methylation of C(1352) in chloroplast 16S rRNA, indicating that CMAL orthologs and this methyl-modification nucleotide is conserved between bacteria and the endosymbiont-derived eukaryotic organelle. The knockout of CMAL in Arabidopsis impairs the chloroplast ribosome accumulation and accordingly reduced the efficiency of mRNA translation. Interestingly, the loss of CMAL leads not only to defects in chloroplast function, but also to abnormal leaf and root development and overall plant morphology. Further investigation showed that CMAL is involved in the plant development probably by modulating auxin derived signaling pathways. This study uncovered the important role of 16S rRNA methylation mediated by CMAL in chloroplast ribosome biogenesis and plant development. |
format | Online Article Text |
id | pubmed-7102989 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-71029892020-04-02 The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development Zou, Meijuan Mu, Ying Chai, Xin Ouyang, Min Yu, Long-Jiang Zhang, Lixin Meurer, Jörg Chi, Wei Nucleic Acids Res Nucleic Acid Enzymes Methylation of nucleotides in ribosomal RNAs (rRNAs) is a ubiquitous feature that occurs in all living organisms. The formation of methylated nucleotides is performed by a variety of RNA-methyltransferases. Chloroplasts of plant cells result from an endosymbiotic event and possess their own genome and ribosomes. However, enzymes responsible for rRNA methylation and the function of modified nucleotides in chloroplasts remain to be determined. Here, we identified an rRNA methyltransferase, CMAL (Chloroplast MraW-Like), in the Arabidopsis chloroplast and investigated its function. CMAL is the Arabidopsis ortholog of bacterial MraW/ RsmH proteins and accounts to the N(4)-methylation of C(1352) in chloroplast 16S rRNA, indicating that CMAL orthologs and this methyl-modification nucleotide is conserved between bacteria and the endosymbiont-derived eukaryotic organelle. The knockout of CMAL in Arabidopsis impairs the chloroplast ribosome accumulation and accordingly reduced the efficiency of mRNA translation. Interestingly, the loss of CMAL leads not only to defects in chloroplast function, but also to abnormal leaf and root development and overall plant morphology. Further investigation showed that CMAL is involved in the plant development probably by modulating auxin derived signaling pathways. This study uncovered the important role of 16S rRNA methylation mediated by CMAL in chloroplast ribosome biogenesis and plant development. Oxford University Press 2020-04-06 2020-02-25 /pmc/articles/PMC7102989/ /pubmed/32095829 http://dx.doi.org/10.1093/nar/gkaa129 Text en © The Author(s) 2020. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Nucleic Acid Enzymes Zou, Meijuan Mu, Ying Chai, Xin Ouyang, Min Yu, Long-Jiang Zhang, Lixin Meurer, Jörg Chi, Wei The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title | The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title_full | The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title_fullStr | The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title_full_unstemmed | The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title_short | The critical function of the plastid rRNA methyltransferase, CMAL, in ribosome biogenesis and plant development |
title_sort | critical function of the plastid rrna methyltransferase, cmal, in ribosome biogenesis and plant development |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7102989/ https://www.ncbi.nlm.nih.gov/pubmed/32095829 http://dx.doi.org/10.1093/nar/gkaa129 |
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