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Locmelis, Roland
Publications (6 of 6) Show all publications
Locmelis, R. (2018). Structural biology studies of thylakoid lumen proteins required for photosystem II assembly and function. (Doctoral dissertation). Umeå: Umeå universitet
Open this publication in new window or tab >>Structural biology studies of thylakoid lumen proteins required for photosystem II assembly and function
2018 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Little is known about the structures and functions of thylakoid lumen proteins. However, some of these proteins have an essential role in photosynthesis. Photosystem II (PSII) complexes are embedded in the thylakoid membrane of oxygenic photosynthetic organisms and one of the central subunits, the D1 protein, is damaged by light during the light driven water – splitting reaction and must be replaced frequently. One of the thylakoid lumen proteins that is essential for assembly and renewal of PSII complexes is the High Chlorophyll Fluorescence 136 (HCF136) protein. Another important protein for the PSII complex assembly is the Low PSII Accumulation Protein 19 (LPA19). Both proteins, HCF136 and LPA19, were shown to bind to the core subunits of the PSII complex from the lumenal side and LPA19 has been shown to explicitly interact with the soluble C-terminus of the D1 protein, one of the core PSII complex proteins. Prior to the replacement of the damaged D1 protein, the PSII complex needs to be disassembled, which is done with the help of the Maintenance of Photosystem II under High light 2 (MPH2) protein. MPH2, also called TL16, is required during the repair cycle of the PSII complex particularly under increased and fluctuating light conditions.

In this work I have determined the three-dimensional X-ray structures of the HCF136 protein at 1.6 Å resolution and the LPA19 protein at 1.2 Å resolution and have also biochemically analyzed possible interactions of HCF136 with the C-termini of D1 protein. In addition, we have determined the NMR structure of the MPH2 protein.

The protein structures of HCF136, LPA19, and MPH2 determined from A. thaliana provide us with a starting point for further studies to improve our understanding of their functional roles in the assembly, maintenance, disassembly and renewal of the PSII complex. The structures are revealing the molecular details that are particularly important during the design of mutations to study protein-protein interactions and the binding of co-factors.

Furthermore, I have contributed to the characterization of AnPrx6, the 1-Cyx peroxiredoxin from Anabaena sp. 7120. Peroxiredoxins are important caretakers of reactive oxygen species and a homolog PrxQ in A.thaliana is found in the thylakoid lumen. The dimeric AnPrx6 protein revealed different active site residues conformations in each of the dimers, which is probably coupled to its enzymatic activity. Unexpectedly, the protein acted also as a chaperone and showed chaperone activity in its dimeric state, which is a novelty for Prx proteins.

Place, publisher, year, edition, pages
Umeå: Umeå universitet, 2018. p. 48
Keywords
structural biology, x-ray crystallography, cloning, protein expression, HCF136, LPA19, MPH2, Prx6, photosynthesis, thylakoid lumen PSII
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-144016 (URN)978-91-7601-807-1 (ISBN)
Public defence
2018-02-05, N430, Naturvetarhuset, Umeå, 10:00 (English)
Opponent
Supervisors
Available from: 2018-01-22 Created: 2018-01-17 Last updated: 2018-06-09Bibliographically approved
Mishra, Y., Hall, M., Locmelis, R., Nam, K., Söderberg, C. A. G., Storm, P., . . . Sauer, U. H. (2017). Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientific Reports, 7, Article ID 17151.
Open this publication in new window or tab >>Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
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2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 17151Article in journal (Refereed) Published
Abstract [en]

Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (C-P) and, if present, the resolving Cys (C-R). A detailed catalytic cycle has been derived for typical 2-Cys Prxs, however, little is known about the catalytic cycle of 1-Cys Prxs. We have characterized Prx6 from the cyanobacterium Anabaena sp. strain PCC7120 (AnPrx6) and found that in addition to the expected peroxidase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to other Prxs. The AnPrx6 crystal structure at 2.3 angstrom resolution reveals different active site conformations in each monomer of the asymmetric obligate homo-dimer. Molecular dynamic simulations support the observed structural plasticity. A FSH motif, conserved in 1-Cys Prxs, precedes the active site PxxxTxxCp signature and might contribute to the 1-Cys Prx reaction cycle.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-143523 (URN)10.1038/s41598-017-17044-3 (DOI)000417354200004 ()29215017 (PubMedID)2-s2.0-85038074530 (Scopus ID)
Note

The original version of this Article contained an error in the title of the paper, where “Anabaena sp. PCC 7120” was incorrectly given as “Anabaena sp. PCC 7210”. This has now been corrected in the PDF and HTML versions of the Article, and in the accompanying Supplementary Information file.

Errata: Author Correction: Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientifc reports. 2018;8:8658. DOI: 10.1038/s41598-018-26715-8

Available from: 2018-01-04 Created: 2018-01-04 Last updated: 2018-06-15Bibliographically approved
Locmelis, R., Stier, G. & Sauer, U. H.Crystal structure of the Photosystem II assembly factor LPA19 from Arabidopsis thaliana at 1.2 Å resolution.
Open this publication in new window or tab >>Crystal structure of the Photosystem II assembly factor LPA19 from Arabidopsis thaliana at 1.2 Å resolution
(English)Manuscript (preprint) (Other academic)
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-144014 (URN)
Available from: 2018-01-17 Created: 2018-01-17 Last updated: 2018-06-09Bibliographically approved
Locmelis, R., Norman, P.-G. & Sauer, U. H.Photosystem II assembly factor LPA19 from Arabidopsis thaliana: Cloning, expression, purification and X-ray diffraction analysis.
Open this publication in new window or tab >>Photosystem II assembly factor LPA19 from Arabidopsis thaliana: Cloning, expression, purification and X-ray diffraction analysis
(English)Manuscript (preprint) (Other academic)
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-144013 (URN)
Available from: 2018-01-17 Created: 2018-01-17 Last updated: 2018-06-09Bibliographically approved
Locmelis, R., Persson, C., Schröder, W. & Sauer, U. H.Solution structure of the Photosystem II repair factor MPH2 from Arabidopsis thaliana: Cloning, expression, purification and structure analysis.
Open this publication in new window or tab >>Solution structure of the Photosystem II repair factor MPH2 from Arabidopsis thaliana: Cloning, expression, purification and structure analysis
(English)Manuscript (preprint) (Other academic)
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-144015 (URN)
Available from: 2018-01-17 Created: 2018-01-17 Last updated: 2018-06-09Bibliographically approved
Locmelis, R., Grundström, C., Storm, P., Murphy, M., Schröder, W. P. & Sauer, U. H.Three-dimensional structure of the Photosystem II assembly factor HCF136 from Arabidopsis thaliana.
Open this publication in new window or tab >>Three-dimensional structure of the Photosystem II assembly factor HCF136 from Arabidopsis thaliana
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(English)Manuscript (preprint) (Other academic)
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-144011 (URN)
Available from: 2018-01-17 Created: 2018-01-17 Last updated: 2018-06-09Bibliographically approved
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