Regulation of translation by methylation multiplicity of 18S rRNA

Kuanqing Liu; Daniel A. Santos; Jeffrey A. Hussmann; Yun Wang; Benjamin M. Sutter; Jonathan S. Weissman; Benjamin P. Tu

doi:10.1016/j.celrep.2021.108825

Regulation of translation by methylation multiplicity of 18S rRNA

Kuanqing Liu, Daniel A. Santos, Jeffrey A. Hussmann, Yun Wang, Benjamin M. Sutter, Jonathan S. Weissman, Benjamin P. Tu

Research output: Contribution to journal › Article › peer-review

14 Scopus citations

Abstract

N⁶-methyladenosine (m⁶A) is a conserved ribonucleoside modification that regulates many facets of RNA metabolism. Using quantitative mass spectrometry, we find that the universally conserved tandem adenosines at the 3′ end of 18S rRNA, thought to be constitutively di-methylated (m⁶₂A), are also mono-methylated (m⁶A). Although present at substoichiometric amounts, m⁶A at these positions increases significantly in response to sulfur starvation in yeast cells and mammalian cell lines. Combining yeast genetics and ribosome profiling, we provide evidence to suggest that m⁶A-bearing ribosomes carry out translation distinctly from m⁶₂A-bearing ribosomes, featuring a striking specificity for sulfur metabolism genes. Our work thus reveals methylation multiplicity as a mechanism to regulate translation.

Original language	English (US)
Article number	108825
Journal	Cell Reports
Volume	34
Issue number	10
DOIs	https://doi.org/10.1016/j.celrep.2021.108825
State	Published - Mar 9 2021

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

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10.1016/j.celrep.2021.108825

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title = "Regulation of translation by methylation multiplicity of 18S rRNA",

abstract = "N6-methyladenosine (m6A) is a conserved ribonucleoside modification that regulates many facets of RNA metabolism. Using quantitative mass spectrometry, we find that the universally conserved tandem adenosines at the 3′ end of 18S rRNA, thought to be constitutively di-methylated (m62A), are also mono-methylated (m6A). Although present at substoichiometric amounts, m6A at these positions increases significantly in response to sulfur starvation in yeast cells and mammalian cell lines. Combining yeast genetics and ribosome profiling, we provide evidence to suggest that m6A-bearing ribosomes carry out translation distinctly from m62A-bearing ribosomes, featuring a striking specificity for sulfur metabolism genes. Our work thus reveals methylation multiplicity as a mechanism to regulate translation.",

author = "Kuanqing Liu and Santos, {Daniel A.} and Hussmann, {Jeffrey A.} and Yun Wang and Sutter, {Benjamin M.} and Weissman, {Jonathan S.} and Tu, {Benjamin P.}",

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T1 - Regulation of translation by methylation multiplicity of 18S rRNA

AU - Liu, Kuanqing

AU - Santos, Daniel A.

AU - Hussmann, Jeffrey A.

AU - Wang, Yun

AU - Sutter, Benjamin M.

AU - Weissman, Jonathan S.

AU - Tu, Benjamin P.

PY - 2021/3/9

Y1 - 2021/3/9

N2 - N6-methyladenosine (m6A) is a conserved ribonucleoside modification that regulates many facets of RNA metabolism. Using quantitative mass spectrometry, we find that the universally conserved tandem adenosines at the 3′ end of 18S rRNA, thought to be constitutively di-methylated (m62A), are also mono-methylated (m6A). Although present at substoichiometric amounts, m6A at these positions increases significantly in response to sulfur starvation in yeast cells and mammalian cell lines. Combining yeast genetics and ribosome profiling, we provide evidence to suggest that m6A-bearing ribosomes carry out translation distinctly from m62A-bearing ribosomes, featuring a striking specificity for sulfur metabolism genes. Our work thus reveals methylation multiplicity as a mechanism to regulate translation.

AB - N6-methyladenosine (m6A) is a conserved ribonucleoside modification that regulates many facets of RNA metabolism. Using quantitative mass spectrometry, we find that the universally conserved tandem adenosines at the 3′ end of 18S rRNA, thought to be constitutively di-methylated (m62A), are also mono-methylated (m6A). Although present at substoichiometric amounts, m6A at these positions increases significantly in response to sulfur starvation in yeast cells and mammalian cell lines. Combining yeast genetics and ribosome profiling, we provide evidence to suggest that m6A-bearing ribosomes carry out translation distinctly from m62A-bearing ribosomes, featuring a striking specificity for sulfur metabolism genes. Our work thus reveals methylation multiplicity as a mechanism to regulate translation.

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Regulation of translation by methylation multiplicity of 18S rRNA

Abstract

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