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Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification
The assembly of large, multi-cofactor membrane protein complexes like photosystem II (PSII) requires a high level of coordination. The process is facilitated by a large network of auxiliary proteins that bind transiently to unassembled subunits, preassembled modules or intermediate states of PSII, w...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458691/ https://www.ncbi.nlm.nih.gov/pubmed/34910272 http://dx.doi.org/10.1007/s11120-021-00891-7 |
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author | Lambertz, Jan Liauw, Pasqual Whitelegge, Julian P. Nowaczyk, Marc M. |
author_facet | Lambertz, Jan Liauw, Pasqual Whitelegge, Julian P. Nowaczyk, Marc M. |
author_sort | Lambertz, Jan |
collection | PubMed |
description | The assembly of large, multi-cofactor membrane protein complexes like photosystem II (PSII) requires a high level of coordination. The process is facilitated by a large network of auxiliary proteins that bind transiently to unassembled subunits, preassembled modules or intermediate states of PSII, which are comprised of a subset of subunits. However, analysis of these immature, partially assembled PSII complexes is hampered by their low abundance and intrinsic instability. In this study, PSII was purified from the thermophilic cyanobacterium Thermosynechococcus elongatus via Twin-Strep-tagged CP43 and further separated by ion exchange chromatography into mature and immature complexes. Mass spectrometry analysis of the immature Psb27-PSII intermediate revealed six different Psb27 proteoforms with distinct lipid modifications. The maturation and functional role of thylakoid localized lipoproteins are discussed. |
format | Online Article Text |
id | pubmed-9458691 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-94586912022-09-10 Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification Lambertz, Jan Liauw, Pasqual Whitelegge, Julian P. Nowaczyk, Marc M. Photosynth Res Original Article The assembly of large, multi-cofactor membrane protein complexes like photosystem II (PSII) requires a high level of coordination. The process is facilitated by a large network of auxiliary proteins that bind transiently to unassembled subunits, preassembled modules or intermediate states of PSII, which are comprised of a subset of subunits. However, analysis of these immature, partially assembled PSII complexes is hampered by their low abundance and intrinsic instability. In this study, PSII was purified from the thermophilic cyanobacterium Thermosynechococcus elongatus via Twin-Strep-tagged CP43 and further separated by ion exchange chromatography into mature and immature complexes. Mass spectrometry analysis of the immature Psb27-PSII intermediate revealed six different Psb27 proteoforms with distinct lipid modifications. The maturation and functional role of thylakoid localized lipoproteins are discussed. Springer Netherlands 2021-12-15 2022 /pmc/articles/PMC9458691/ /pubmed/34910272 http://dx.doi.org/10.1007/s11120-021-00891-7 Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/Open AccessThis 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/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Original Article Lambertz, Jan Liauw, Pasqual Whitelegge, Julian P. Nowaczyk, Marc M. Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title | Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title_full | Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title_fullStr | Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title_full_unstemmed | Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title_short | Mass spectrometry analysis of the photosystem II assembly factor Psb27 revealed variations in its lipid modification |
title_sort | mass spectrometry analysis of the photosystem ii assembly factor psb27 revealed variations in its lipid modification |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9458691/ https://www.ncbi.nlm.nih.gov/pubmed/34910272 http://dx.doi.org/10.1007/s11120-021-00891-7 |
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