Eukaryotic wobble uridine modifications promote a functionally redundant decoding system
(2008) In Molecular and Cellular Biology 28(10). p.12-3301- Abstract
The translational decoding properties of tRNAs are modulated by naturally occurring modifications of their nucleosides. Uridines located at the wobble position (nucleoside 34 [U(34)]) in eukaryotic cytoplasmic tRNAs often harbor a 5-methoxycarbonylmethyl (mcm(5)) or a 5-carbamoylmethyl (ncm(5)) side chain and sometimes an additional 2-thio (s(2)) or 2'-O-methyl group. Although a variety of models explaining the role of these modifications have been put forth, their in vivo functions have not been defined. In this study, we utilized recently characterized modification-deficient Saccharomyces cerevisiae cells to test the wobble rules in vivo. We show that mcm(5) and ncm(5) side chains promote decoding of G-ending codons and that... (More)
The translational decoding properties of tRNAs are modulated by naturally occurring modifications of their nucleosides. Uridines located at the wobble position (nucleoside 34 [U(34)]) in eukaryotic cytoplasmic tRNAs often harbor a 5-methoxycarbonylmethyl (mcm(5)) or a 5-carbamoylmethyl (ncm(5)) side chain and sometimes an additional 2-thio (s(2)) or 2'-O-methyl group. Although a variety of models explaining the role of these modifications have been put forth, their in vivo functions have not been defined. In this study, we utilized recently characterized modification-deficient Saccharomyces cerevisiae cells to test the wobble rules in vivo. We show that mcm(5) and ncm(5) side chains promote decoding of G-ending codons and that concurrent mcm(5) and s(2) groups improve reading of both A- and G-ending codons. Moreover, the observation that the mcm(5)U(34)- and some ncm(5)U(34)-containing tRNAs efficiently read G-ending codons challenges the notion that eukaryotes do not use U-G wobbling.
(Less)
- author
- Johansson, Marcus J O LU ; Esberg, Anders ; Huang, Bo ; Björk, Glenn R and Byström, Anders S
- publishing date
- 2008-05
- type
- Contribution to journal
- publication status
- published
- keywords
- Anticodon/chemistry, Base Sequence, Codon/genetics, Genes, Fungal, Plasmids/genetics, Protein Biosynthesis, RNA, Fungal/chemistry, RNA, Transfer/chemistry, Saccharomyces cerevisiae/genetics, Transfer RNA Aminoacylation, Uridine/chemistry
- in
- Molecular and Cellular Biology
- volume
- 28
- issue
- 10
- pages
- 12 - 3301
- publisher
- Taylor & Francis
- external identifiers
-
- pmid:18332122
- scopus:43249104840
- ISSN
- 0270-7306
- DOI
- 10.1128/MCB.01542-07
- language
- English
- LU publication?
- no
- id
- 4eef4dce-1fd3-45f8-818c-692e46109679
- date added to LUP
- 2024-03-05 16:51:01
- date last changed
- 2025-10-18 21:20:06
@article{4eef4dce-1fd3-45f8-818c-692e46109679,
abstract = {{<p>The translational decoding properties of tRNAs are modulated by naturally occurring modifications of their nucleosides. Uridines located at the wobble position (nucleoside 34 [U(34)]) in eukaryotic cytoplasmic tRNAs often harbor a 5-methoxycarbonylmethyl (mcm(5)) or a 5-carbamoylmethyl (ncm(5)) side chain and sometimes an additional 2-thio (s(2)) or 2'-O-methyl group. Although a variety of models explaining the role of these modifications have been put forth, their in vivo functions have not been defined. In this study, we utilized recently characterized modification-deficient Saccharomyces cerevisiae cells to test the wobble rules in vivo. We show that mcm(5) and ncm(5) side chains promote decoding of G-ending codons and that concurrent mcm(5) and s(2) groups improve reading of both A- and G-ending codons. Moreover, the observation that the mcm(5)U(34)- and some ncm(5)U(34)-containing tRNAs efficiently read G-ending codons challenges the notion that eukaryotes do not use U-G wobbling.</p>}},
author = {{Johansson, Marcus J O and Esberg, Anders and Huang, Bo and Björk, Glenn R and Byström, Anders S}},
issn = {{0270-7306}},
keywords = {{Anticodon/chemistry; Base Sequence; Codon/genetics; Genes, Fungal; Plasmids/genetics; Protein Biosynthesis; RNA, Fungal/chemistry; RNA, Transfer/chemistry; Saccharomyces cerevisiae/genetics; Transfer RNA Aminoacylation; Uridine/chemistry}},
language = {{eng}},
number = {{10}},
pages = {{12--3301}},
publisher = {{Taylor & Francis}},
series = {{Molecular and Cellular Biology}},
title = {{Eukaryotic wobble uridine modifications promote a functionally redundant decoding system}},
url = {{http://dx.doi.org/10.1128/MCB.01542-07}},
doi = {{10.1128/MCB.01542-07}},
volume = {{28}},
year = {{2008}},
}