How Elongator Acetylates tRNA Bases
Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U<sub>34</sub>) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation...
Main Authors: | , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2020-11-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | https://www.mdpi.com/1422-0067/21/21/8209 |
id |
doaj-d224989d93b749ca8803475c1faa4c86 |
---|---|
record_format |
Article |
spelling |
doaj-d224989d93b749ca8803475c1faa4c862020-11-25T03:59:24ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-11-01218209820910.3390/ijms21218209How Elongator Acetylates tRNA BasesNour-el-Hana Abbassi0Anna Biela1Sebastian Glatt2Ting-Yu Lin3Malopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, PolandMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, PolandMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, PolandMalopolska Centre of Biotechnology, Jagiellonian University, 30-387 Kraków, PolandElp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U<sub>34</sub>) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation elongation rates and directly links acetyl-CoA metabolism to both protein synthesis rates and the proteome integrity. Of note, several human diseases, including various cancers and neurodegenerative disorders, correlate with the dysregulation of Elongator’s tRNA modification activity. In this review, we focus on recent findings regarding the structure of Elp3 and the role of acetyl-CoA during its unique modification reaction.https://www.mdpi.com/1422-0067/21/21/8209ElongatorElp3tRNA modificationacetyl-CoAproteome balancecancers |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Nour-el-Hana Abbassi Anna Biela Sebastian Glatt Ting-Yu Lin |
spellingShingle |
Nour-el-Hana Abbassi Anna Biela Sebastian Glatt Ting-Yu Lin How Elongator Acetylates tRNA Bases International Journal of Molecular Sciences Elongator Elp3 tRNA modification acetyl-CoA proteome balance cancers |
author_facet |
Nour-el-Hana Abbassi Anna Biela Sebastian Glatt Ting-Yu Lin |
author_sort |
Nour-el-Hana Abbassi |
title |
How Elongator Acetylates tRNA Bases |
title_short |
How Elongator Acetylates tRNA Bases |
title_full |
How Elongator Acetylates tRNA Bases |
title_fullStr |
How Elongator Acetylates tRNA Bases |
title_full_unstemmed |
How Elongator Acetylates tRNA Bases |
title_sort |
how elongator acetylates trna bases |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-11-01 |
description |
Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U<sub>34</sub>) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation elongation rates and directly links acetyl-CoA metabolism to both protein synthesis rates and the proteome integrity. Of note, several human diseases, including various cancers and neurodegenerative disorders, correlate with the dysregulation of Elongator’s tRNA modification activity. In this review, we focus on recent findings regarding the structure of Elp3 and the role of acetyl-CoA during its unique modification reaction. |
topic |
Elongator Elp3 tRNA modification acetyl-CoA proteome balance cancers |
url |
https://www.mdpi.com/1422-0067/21/21/8209 |
work_keys_str_mv |
AT nourelhanaabbassi howelongatoracetylatestrnabases AT annabiela howelongatoracetylatestrnabases AT sebastianglatt howelongatoracetylatestrnabases AT tingyulin howelongatoracetylatestrnabases |
_version_ |
1724454196391968768 |