Author
Listed:
- Chen Xiao
(Hong Kong Baptist University)
- Kaien Li
(Hong Kong Baptist University)
- Jingmin Hua
(Hong Kong Baptist University)
- Zhao He
(Hong Kong Baptist University)
- Feng Zhang
(Hong Kong Baptist University)
- Qiongfang Li
(Hong Kong Baptist University)
- Hailei Zhang
(Hong Kong Baptist University)
- Lei Yang
(The Chinese University of Hong Kong)
- Shuying Pan
(Hong Kong Baptist University)
- Zongwei Cai
(Hong Kong Baptist University)
- Zhiling Yu
(Hong Kong Baptist University)
- Kam-Bo Wong
(The Chinese University of Hong Kong)
- Yiji Xia
(Hong Kong Baptist University
Hong Kong Baptist University
The Chinese University of Hong Kong)
Abstract
Eukaryotic messenger RNA (mRNA) typically contains a methylated guanosine (m7G) cap, which mediates major steps of mRNA metabolism. Recently, some RNAs in both prokaryotic and eukaryotic organisms have been found to carry a non-canonical cap such as the NAD cap. Here we report that Arabidopsis DXO family protein AtDXO1, which was previously known to be a decapping enzyme for NAD-capped RNAs (NAD-RNA), is an essential component for m7G capping. AtDXO1 associates with and activates RNA guanosine-7 methyltransferase (AtRNMT1) to catalyze conversion of the guanosine cap to the m7G cap. AtRNMT1 is an essential gene. Partial loss-of-function mutations of AtRNMT1 and knockout mutation of AtDXO1 reduce m7G-capped mRNA but increase G-capped mRNAs, leading to similar pleiotropic phenotypes, whereas overexpression of AtRNMT1 partially restores the atdxo1 phenotypes. This work reveals an important mechanism in m7G capping in plants by which the NAD-RNA decapping enzyme AtDXO1 is required for efficient guanosine cap methylation.
Suggested Citation
Chen Xiao & Kaien Li & Jingmin Hua & Zhao He & Feng Zhang & Qiongfang Li & Hailei Zhang & Lei Yang & Shuying Pan & Zongwei Cai & Zhiling Yu & Kam-Bo Wong & Yiji Xia, 2023.
"Arabidopsis DXO1 activates RNMT1 to methylate the mRNA guanosine cap,"
Nature Communications, Nature, vol. 14(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-35903-8
DOI: 10.1038/s41467-023-35903-8
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