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Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum
Many filamentous fungi produce plant-polysaccharide-degrading enzymes (PPDE); however, the regulatory mechanism of this process is poorly understood. A Gal4-like transcription factor, CxrA, is essential for mycelial growth and PPDE production in Penicillium oxalicum. Its N-terminal region, CxrA(Δ207...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Public Library of Science
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10414604/ https://www.ncbi.nlm.nih.gov/pubmed/37523410 http://dx.doi.org/10.1371/journal.pgen.1010867 |
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author | Zhao, Shuai Mo, Li-Xiang Li, Wen-Tong Jiang, Lian-Li Meng, Yi-Yuan Ou, Jian-Feng Liao, Lu-Sheng Yan, Yu-Si Luo, Xue-Mei Feng, Jia-Xun |
author_facet | Zhao, Shuai Mo, Li-Xiang Li, Wen-Tong Jiang, Lian-Li Meng, Yi-Yuan Ou, Jian-Feng Liao, Lu-Sheng Yan, Yu-Si Luo, Xue-Mei Feng, Jia-Xun |
author_sort | Zhao, Shuai |
collection | PubMed |
description | Many filamentous fungi produce plant-polysaccharide-degrading enzymes (PPDE); however, the regulatory mechanism of this process is poorly understood. A Gal4-like transcription factor, CxrA, is essential for mycelial growth and PPDE production in Penicillium oxalicum. Its N-terminal region, CxrA(Δ207–733) is required for the regulatory functions of whole CxrA, and contains a DNA-binding domain (CxrA(Δ1–16&Δ59–733)) and a methylated arginine (R) 94. Methylation of R94 is mediated by an arginine N-methyltransferase, PRMT2 and appears to induce dimerization of CxrA(Δ1–60). Overexpression of prmt2 in P. oxalicum increases PPDE production by 41.4–95.1% during growth on Avicel, compared with the background strain Δku70;hph(R+). Another arginine N-methyltransferase, PRMT3, appears to assist entry of CxrA into the nucleus, and interacts with CxrA(Δ1–60) in vitro under Avicel induction. Deletion of prmt3 resulted in 67.0–149.7% enhanced PPDE production by P. oxalicum. These findings provide novel insights into the regulatory mechanism of fungal PPDE production. |
format | Online Article Text |
id | pubmed-10414604 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-104146042023-08-11 Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum Zhao, Shuai Mo, Li-Xiang Li, Wen-Tong Jiang, Lian-Li Meng, Yi-Yuan Ou, Jian-Feng Liao, Lu-Sheng Yan, Yu-Si Luo, Xue-Mei Feng, Jia-Xun PLoS Genet Research Article Many filamentous fungi produce plant-polysaccharide-degrading enzymes (PPDE); however, the regulatory mechanism of this process is poorly understood. A Gal4-like transcription factor, CxrA, is essential for mycelial growth and PPDE production in Penicillium oxalicum. Its N-terminal region, CxrA(Δ207–733) is required for the regulatory functions of whole CxrA, and contains a DNA-binding domain (CxrA(Δ1–16&Δ59–733)) and a methylated arginine (R) 94. Methylation of R94 is mediated by an arginine N-methyltransferase, PRMT2 and appears to induce dimerization of CxrA(Δ1–60). Overexpression of prmt2 in P. oxalicum increases PPDE production by 41.4–95.1% during growth on Avicel, compared with the background strain Δku70;hph(R+). Another arginine N-methyltransferase, PRMT3, appears to assist entry of CxrA into the nucleus, and interacts with CxrA(Δ1–60) in vitro under Avicel induction. Deletion of prmt3 resulted in 67.0–149.7% enhanced PPDE production by P. oxalicum. These findings provide novel insights into the regulatory mechanism of fungal PPDE production. Public Library of Science 2023-07-31 /pmc/articles/PMC10414604/ /pubmed/37523410 http://dx.doi.org/10.1371/journal.pgen.1010867 Text en © 2023 Zhao et al https://creativecommons.org/licenses/by/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Article Zhao, Shuai Mo, Li-Xiang Li, Wen-Tong Jiang, Lian-Li Meng, Yi-Yuan Ou, Jian-Feng Liao, Lu-Sheng Yan, Yu-Si Luo, Xue-Mei Feng, Jia-Xun Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title | Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title_full | Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title_fullStr | Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title_full_unstemmed | Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title_short | Arginine methyltransferases PRMT2 and PRMT3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in Penicillium oxalicum |
title_sort | arginine methyltransferases prmt2 and prmt3 are essential for biosynthesis of plant-polysaccharide-degrading enzymes in penicillium oxalicum |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10414604/ https://www.ncbi.nlm.nih.gov/pubmed/37523410 http://dx.doi.org/10.1371/journal.pgen.1010867 |
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