Evidence map›Paper›PMID 25511433›Full record

ArticlePlant physiology2015

PHOTOSYSTEM II PROTEIN33, a protein conserved in the plastid lineage, is associated with the chloroplast thylakoid membrane and provides stability to photosystem II supercomplexes in Arabidopsis.

Rikard Fristedt, Andrei Herdean, Crysten E Blaby-Haas, Fikret Mamedov, Sabeeha S Merchant, Robert L Last, Björn Lundin

Erratum issuedAbstract read
In one paragraph

Article in Plant physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed.

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  9. Transcriptome Analysis of Air Space-Type Variegation Formation inInternational journal of molecular sciences · 2022
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  20. Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Rikard FristedtDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).
Andrei HerdeanDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).
Crysten E Blaby-HaasDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).
Fikret MamedovDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).
Sabeeha S MerchantDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).ORCID http://orcid.org/0000-0002-2594-509X
Robert L LastDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.).ORCID http://orcid.org/0000-0001-6974-9587
Björn LundinDepartment of Chemistry and Biochemistry (R.F., C.E.B.-H., S.S.M.) and Institute for Genomics and Proteomics (S.S.M.), University of California, Los Angeles, California 90095;Department of Biological and Environmental Sciences, University of Gothenburg, 405 30 Gothenburg, Sweden (A.H., B.L.);Department of Chemistry, Ångström Laboratory, Uppsala University, 751 20 Uppsala, Sweden (F.M.); andDepartment of Biochemistry and Molecular Biology and Department of Plant Biology, Michigan State University, East Lansing, Michigan 48824 (R.L.L., B.L.) bjorn.lundin@gmail.com.

Funding

Dissection of the Molecular Details of Fe Deficiency AcclimationF32GM100753 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BLABY, CRYSTEN ELIZABETH · 2012 to 2014
$156k
NIGMS NIH HHS F32 GM100753NIGMS NIH HHS GM100753
6 · The paper itself

Abstract

Photosystem II (PSII) is a multiprotein complex that catalyzes the light-driven water-splitting reactions of oxygenic photosynthesis. Light absorption by PSII leads to the production of excited states and reactive oxygen species that can cause damage to this complex. Here, we describe Arabidopsis (Arabidopsis thaliana) At1g71500, which encodes a previously uncharacterized protein that is a PSII auxiliary core protein and hence is named PHOTOSYSTEM II PROTEIN33 (PSB33). We present evidence that PSB33 functions in the maintenance of PSII-light-harvesting complex II (LHCII) supercomplex organization. PSB33 encodes a protein with a chloroplast transit peptide and one transmembrane segment. In silico analysis of PSB33 revealed a light-harvesting complex-binding motif within the transmembrane segment and a large surface-exposed head domain. Biochemical analysis of PSII complexes further indicates that PSB33 is an integral membrane protein located in the vicinity of LHCII and the PSII CP43 reaction center protein. Phenotypic characterization of mutants lacking PSB33 revealed reduced amounts of PSII-LHCII supercomplexes, very low state transition, and a lower capacity for nonphotochemical quenching, leading to increased photosensitivity in the mutant plants under light stress. Taken together, these results suggest a role for PSB33 in regulating and optimizing photosynthesis in response to changing light levels.

Indexed as

Conserved SequenceArabidopsisArabidopsis ProteinsChlorophyllFluorescenceGenes, PlantIntracellular MembranesLightLight-Harvesting Protein ComplexesMembrane ProteinsMutationPhenotypePhotochemical ProcessesPhotosystem II Protein ComplexProtein StabilityProtein TransportArabidopsis ProteinsChlorophyllLight-Harvesting Protein ComplexesMembrane ProteinsPhotosystem II Protein Complex

Identifiers

PMID25511433
PMCPMC4326745

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.