Journal article
Recombinant expression and subcellular targeting of the particulate methane monooxygenase (pMMO) protein components in plants
- Abstract:
-
Methane is a potent greenhouse gas, which has contributed to approximately a fifth of global warming since pre-industrial times. The agricultural sector produces significant methane emissions, especially from livestock, waste management and rice cultivation. Rice fields alone generate around 9% of total anthropogenic emissions. Methane is produced in waterlogged paddy fields by methanogenic archaea, and transported to the atmosphere through the aerenchyma tissue of rice plants. Thus, bioengineering rice with catalysts to detoxify methane en route could contribute to an efficient emission mitigation strategy. Particulate methane monooxygenase (pMMO) is the predominant methane catalyst found in nature, and is an enzyme complex expressed by methanotrophic bacteria. Recombinant expression of pMMO has been challenging, potentially due to its membrane localization, multimeric structure, and polycistronic operon. Here we show the first steps towards the engineering of plants for methane detoxification with the three pMMO subunits expressed in the model systems tobacco and Arabidopsis. Membrane topology and protein–protein interactions were consistent with correct folding and assembly of the pMMO subunits on the plant ER. Moreover, a synthetic self-cleaving polypeptide resulted in simultaneous expression of all three subunits, although low expression levels precluded more detailed structural investigation. The work presents plant cells as a novel heterologous system for pMMO allowing for protein expression and modification.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
Actions
Access Document
- Files:
-
-
(Preview, Version of record, pdf, 4.1MB, Terms of use)
-
- Publisher copy:
- 10.1038/s41598-023-42224-9
Authors
- Grant:
- BB/R014086/1
- BB/W011166/1
- Publisher:
- Springer Nature
- Journal:
- Scientific Reports More from this journal
- Volume:
- 13
- Article number:
- 15337
- Publication date:
- 2023-09-15
- Acceptance date:
- 2023-09-07
- DOI:
- EISSN:
-
2045-2322
- Pmid:
-
37714899
- Language:
-
English
- Keywords:
- Pubs id:
-
1533754
- Local pid:
-
pubs:1533754
- Deposit date:
-
2023-10-06
Terms of use
- Copyright holder:
- Springer Nature Limited
- Copyright date:
- 2023
- Rights statement:
- Copyright © 2023, Springer Nature Limited. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.
- Licence:
- CC Attribution (CC BY)
If you are the owner of this record, you can report an update to it here: Report update to this record