|
Protein Arginine Methyltransferase 3 Fine-tunes the Assembly/Disassembly of Pre-Ribosome to Repress Nucleolar Stress by Interacting with RPS2B in Arabidopsis
Runlai Hang, Zhen Wang, Chao Yang, Lilan Luo, Beixin Mo, Xuemei Chen, Jing Sun, Chunyan Liu, XiaofengCao
Molecular Plant
Abstract
Ribosome biogenesis, taking place mainly in the nucleolus, involves coordinated expression of pre-ribosomal RNAs (pre-rRNAs) and ribosomal proteins, pre-rRNA processing, and subunit assembly with the aid of numerous assembly factors. Our previous study showed that the Arabidopsis thaliana protein arginine methyltransferase AtPRMT3 regulates pre-rRNA processing; however, the molecular mechanism remains unknown. Here we report that AtPRMT3 interacts with Ribosomal Protein S2 (RPS2) facilitating the 90S/Small Subunit (SSU) processome processing and repressing nucleolar stress. We isolated an intragenic suppressor of atprmt3-2 bearing the entire N-terminus but lacking an intact enzymatic activity domain of AtPRMT3, which rescued the developmental defects of atprmt3-2. RPS2 was further identified as an interacting partner of AtPRMT3, and loss-of-function rps2a2b mutants were reminiscent of atprmt3 phenotypically, including pleiotropic developmental defects and aberrant pre-rRNA processing. RPS2B bound directly to pre-rRNAs in the nucleus, and such binding was enhanced in atprmt3-2. Consistently, multiple components of 90S/SSU processome were more enriched by RPS2B in atprmt3-2, which causes early pre-rRNA processing defects and nucleolar stress. Our study uncovered a novel mechanism by which AtPRMT3 cooperates with RPS2B to facilitate the dynamic assembly/disassembly of the 90S/SSU processome during ribosome biogenesis and repress nucleolar stress.
|
Paper Code |
DOI:10.1016/j.molp.2020.10.006 |
Title |
Protein Arginine Methyltransferase 3 Fine-tunes the Assembly/Disassembly of Pre-Ribosome to Repress Nucleolar Stress by Interacting with RPS2B in Arabidopsis |
Authors |
Runlai Hang, Zhen Wang, Chao Yang, Lilan Luo, Beixin Mo, Xuemei Chen, Jing Sun, Chunyan Liu, XiaofengCao |
Corresponding Author |
|
Year |
2020-10-20 |
Title of Journal |
|
Volume |
|
Number |
|
Page |
|
Abstract |
Ribosome biogenesis, taking place mainly in the nucleolus, involves coordinated expression of pre-ribosomal RNAs (pre-rRNAs) and ribosomal proteins, pre-rRNA processing, and subunit assembly with the aid of numerous assembly factors. Our previous study showed that the Arabidopsis thaliana protein arginine methyltransferase AtPRMT3 regulates pre-rRNA processing; however, the molecular mechanism remains unknown. Here we report that AtPRMT3 interacts with Ribosomal Protein S2 (RPS2) facilitating the 90S/Small Subunit (SSU) processome processing and repressing nucleolar stress. We isolated an intragenic suppressor of atprmt3-2 bearing the entire N-terminus but lacking an intact enzymatic activity domain of AtPRMT3, which rescued the developmental defects of atprmt3-2. RPS2 was further identified as an interacting partner of AtPRMT3, and loss-of-function rps2a2b mutants were reminiscent of atprmt3 phenotypically, including pleiotropic developmental defects and aberrant pre-rRNA processing. RPS2B bound directly to pre-rRNAs in the nucleus, and such binding was enhanced in atprmt3-2. Consistently, multiple components of 90S/SSU processome were more enriched by RPS2B in atprmt3-2, which causes early pre-rRNA processing defects and nucleolar stress. Our study uncovered a novel mechanism by which AtPRMT3 cooperates with RPS2B to facilitate the dynamic assembly/disassembly of the 90S/SSU processome during ribosome biogenesis and repress nucleolar stress. |
Full Text |
|
Full Text Link |
|
Others: |
Ribosome biogenesis, taking place mainly in the nucleolus, involves coordinated expression of pre-ribosomal RNAs (pre-rRNAs) and ribosomal proteins, pre-rRNA processing, and subunit assembly with the aid of numerous assembly factors. Our previous study showed that the Arabidopsis thaliana protein arginine methyltransferase AtPRMT3 regulates pre-rRNA processing; however, the molecular mechanism remains unknown. Here we report that AtPRMT3 interacts with Ribosomal Protein S2 (RPS2) facilitating the 90S/Small Subunit (SSU) processome processing and repressing nucleolar stress. We isolated an intragenic suppressor of atprmt3-2 bearing the entire N-terminus but lacking an intact enzymatic activity domain of AtPRMT3, which rescued the developmental defects of atprmt3-2. RPS2 was further identified as an interacting partner of AtPRMT3, and loss-of-function rps2a2b mutants were reminiscent of atprmt3 phenotypically, including pleiotropic developmental defects and aberrant pre-rRNA processing. RPS2B bound directly to pre-rRNAs in the nucleus, and such binding was enhanced in atprmt3-2. Consistently, multiple components of 90S/SSU processome were more enriched by RPS2B in atprmt3-2, which causes early pre-rRNA processing defects and nucleolar stress. Our study uncovered a novel mechanism by which AtPRMT3 cooperates with RPS2B to facilitate the dynamic assembly/disassembly of the 90S/SSU processome during ribosome biogenesis and repress nucleolar stress. |
Classification: |
|
Source: |
|
|
|