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Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10
Ribosome biogenesis is one of the most energy demanding processes in the cell. In eukaryotes, the main steps of this process occur in the nucleolus and include pre-ribosomal RNA (pre-rRNA) processing, post-transcriptional modifications, and assembly of many non-ribosomal factors and ribosomal protei...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6770127/ https://www.ncbi.nlm.nih.gov/pubmed/31491951 http://dx.doi.org/10.3390/cells8091035 |
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author | Sleiman, Sophie Dragon, Francois |
author_facet | Sleiman, Sophie Dragon, Francois |
author_sort | Sleiman, Sophie |
collection | PubMed |
description | Ribosome biogenesis is one of the most energy demanding processes in the cell. In eukaryotes, the main steps of this process occur in the nucleolus and include pre-ribosomal RNA (pre-rRNA) processing, post-transcriptional modifications, and assembly of many non-ribosomal factors and ribosomal proteins in order to form mature and functional ribosomes. In yeast and humans, the nucleolar RNA acetyltransferase Kre33/NAT10 participates in different maturation events, such as acetylation and processing of 18S rRNA, and assembly of the 40S ribosomal subunit. Here, we review the structural and functional features of Kre33/NAT10 RNA acetyltransferase, and we underscore the importance of this enzyme in ribosome biogenesis, as well as in acetylation of non-ribosomal targets. We also report on the role of human NAT10 in Hutchinson–Gilford progeria syndrome. |
format | Online Article Text |
id | pubmed-6770127 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-67701272019-10-30 Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 Sleiman, Sophie Dragon, Francois Cells Review Ribosome biogenesis is one of the most energy demanding processes in the cell. In eukaryotes, the main steps of this process occur in the nucleolus and include pre-ribosomal RNA (pre-rRNA) processing, post-transcriptional modifications, and assembly of many non-ribosomal factors and ribosomal proteins in order to form mature and functional ribosomes. In yeast and humans, the nucleolar RNA acetyltransferase Kre33/NAT10 participates in different maturation events, such as acetylation and processing of 18S rRNA, and assembly of the 40S ribosomal subunit. Here, we review the structural and functional features of Kre33/NAT10 RNA acetyltransferase, and we underscore the importance of this enzyme in ribosome biogenesis, as well as in acetylation of non-ribosomal targets. We also report on the role of human NAT10 in Hutchinson–Gilford progeria syndrome. MDPI 2019-09-05 /pmc/articles/PMC6770127/ /pubmed/31491951 http://dx.doi.org/10.3390/cells8091035 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Sleiman, Sophie Dragon, Francois Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title | Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title_full | Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title_fullStr | Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title_full_unstemmed | Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title_short | Recent Advances on the Structure and Function of RNA Acetyltransferase Kre33/NAT10 |
title_sort | recent advances on the structure and function of rna acetyltransferase kre33/nat10 |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6770127/ https://www.ncbi.nlm.nih.gov/pubmed/31491951 http://dx.doi.org/10.3390/cells8091035 |
work_keys_str_mv | AT sleimansophie recentadvancesonthestructureandfunctionofrnaacetyltransferasekre33nat10 AT dragonfrancois recentadvancesonthestructureandfunctionofrnaacetyltransferasekre33nat10 |