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Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation
Plastoglobules are lipoprotein particles that are found in different types of plastids. They contain a very specific and specialized set of lipids and proteins. Plastoglobules are highly dynamic in size and shape, and are therefore thought to participate in adaptation processes during either abiotic...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6685665/ https://www.ncbi.nlm.nih.gov/pubmed/30976809 http://dx.doi.org/10.1093/jxb/erz177 |
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author | Espinoza-Corral, Roberto Heinz, Steffen Klingl, Andreas Jahns, Peter Lehmann, Martin Meurer, Jörg Nickelsen, Jörg Soll, Jürgen Schwenkert, Serena |
author_facet | Espinoza-Corral, Roberto Heinz, Steffen Klingl, Andreas Jahns, Peter Lehmann, Martin Meurer, Jörg Nickelsen, Jörg Soll, Jürgen Schwenkert, Serena |
author_sort | Espinoza-Corral, Roberto |
collection | PubMed |
description | Plastoglobules are lipoprotein particles that are found in different types of plastids. They contain a very specific and specialized set of lipids and proteins. Plastoglobules are highly dynamic in size and shape, and are therefore thought to participate in adaptation processes during either abiotic or biotic stresses or transitions between developmental stages. They are suggested to function in thylakoid biogenesis, isoprenoid metabolism, and chlorophyll degradation. While several plastoglobular proteins contain identifiable domains, others provide no structural clues to their function. In this study, we investigate the role of plastoglobular protein 18 (PG18), which is conserved from cyanobacteria to higher plants. Analysis of a PG18 loss-of-function mutant in Arabidopsis thaliana demonstrated that PG18 plays an important role in thylakoid formation; the loss of PG18 results in impaired accumulation, assembly, and function of thylakoid membrane complexes. Interestingly, the mutant accumulated less chlorophyll and carotenoids, whereas xanthophyll cycle pigments were increased. Accumulation of photosynthetic complexes is similarly affected in both a Synechocystis and an Arabidopsis PG18 mutant. However, the ultrastructure of cyanobacterial thylakoids is not compromised by the lack of PG18, probably due to its less complex architecture. |
format | Online Article Text |
id | pubmed-6685665 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-66856652019-08-12 Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation Espinoza-Corral, Roberto Heinz, Steffen Klingl, Andreas Jahns, Peter Lehmann, Martin Meurer, Jörg Nickelsen, Jörg Soll, Jürgen Schwenkert, Serena J Exp Bot Research Papers Plastoglobules are lipoprotein particles that are found in different types of plastids. They contain a very specific and specialized set of lipids and proteins. Plastoglobules are highly dynamic in size and shape, and are therefore thought to participate in adaptation processes during either abiotic or biotic stresses or transitions between developmental stages. They are suggested to function in thylakoid biogenesis, isoprenoid metabolism, and chlorophyll degradation. While several plastoglobular proteins contain identifiable domains, others provide no structural clues to their function. In this study, we investigate the role of plastoglobular protein 18 (PG18), which is conserved from cyanobacteria to higher plants. Analysis of a PG18 loss-of-function mutant in Arabidopsis thaliana demonstrated that PG18 plays an important role in thylakoid formation; the loss of PG18 results in impaired accumulation, assembly, and function of thylakoid membrane complexes. Interestingly, the mutant accumulated less chlorophyll and carotenoids, whereas xanthophyll cycle pigments were increased. Accumulation of photosynthetic complexes is similarly affected in both a Synechocystis and an Arabidopsis PG18 mutant. However, the ultrastructure of cyanobacterial thylakoids is not compromised by the lack of PG18, probably due to its less complex architecture. Oxford University Press 2019-08-01 2019-04-12 /pmc/articles/PMC6685665/ /pubmed/30976809 http://dx.doi.org/10.1093/jxb/erz177 Text en © The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Research Papers Espinoza-Corral, Roberto Heinz, Steffen Klingl, Andreas Jahns, Peter Lehmann, Martin Meurer, Jörg Nickelsen, Jörg Soll, Jürgen Schwenkert, Serena Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title | Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title_full | Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title_fullStr | Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title_full_unstemmed | Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title_short | Plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
title_sort | plastoglobular protein 18 is involved in chloroplast function and thylakoid formation |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6685665/ https://www.ncbi.nlm.nih.gov/pubmed/30976809 http://dx.doi.org/10.1093/jxb/erz177 |
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