Cargando…

Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases

Last step of electron transport from ferredoxin to NADP+ in photosynthesis light reactions catalyses ferredoxin: NADP(+) oxidoreductase (FNR). FNR is present as soluble protein in stroma, but also bound to the protein complexes on the membrane with thylakoid rhodanase-like protein (TROL) and translo...

Descripción completa

Detalles Bibliográficos
Autores principales: Rac, Anja, Fulgosi, Hrvoje
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6953530/
https://www.ncbi.nlm.nih.gov/pubmed/31938718
http://dx.doi.org/10.1016/j.dib.2019.105038
_version_ 1783486641621434368
author Rac, Anja
Fulgosi, Hrvoje
author_facet Rac, Anja
Fulgosi, Hrvoje
author_sort Rac, Anja
collection PubMed
description Last step of electron transport from ferredoxin to NADP+ in photosynthesis light reactions catalyses ferredoxin: NADP(+) oxidoreductase (FNR). FNR is present as soluble protein in stroma, but also bound to the protein complexes on the membrane with thylakoid rhodanase-like protein (TROL) and translocon on the inner envelope chloroplast membrane (Tic62), which have identical C terminal FNR binding domain [1,2]. During the electron transport, FNR anchored by TROL protein transfers electrons on NADP+ and forms NADPH which is then used in Calvin cycle as reducing agent. TROL is an integral membrane protein [3] with an inactive rhodanase-like domain (RHO) facing stroma which, as proposed earlier [4], could bind a small ligand leading to releasing or binding of FNR. FNR-TROL protein complex is necessary for optimal photosynthetic electron flow [1]. It has been shown that C4 plant maize FNR isomers have different N-terminal structure which determines binding affinity to protein complexes and different ratios of bound and unbound FNR in bundle sheath and mesophyll cells, depending on preferable photosynthetic electron transport [5]. Mutant Arabidopsis plant that contain maize FNR1 protein showed influence on dynamic association of FNR and change in excitation balance between photosystems which then influenced photo induced electron transport and finally photosynthesis [5]. In order to determine the influence of maize FNR1 on photosynthesis in C3 plants and difference in interaction strength with TROL, we preformed Yeast two hybrid screening, x-alpha-gal assay and β-galactosidase assay.
format Online
Article
Text
id pubmed-6953530
institution National Center for Biotechnology Information
language English
publishDate 2019
publisher Elsevier
record_format MEDLINE/PubMed
spelling pubmed-69535302020-01-14 Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases Rac, Anja Fulgosi, Hrvoje Data Brief Genetics, Genomics and Molecular Biology Last step of electron transport from ferredoxin to NADP+ in photosynthesis light reactions catalyses ferredoxin: NADP(+) oxidoreductase (FNR). FNR is present as soluble protein in stroma, but also bound to the protein complexes on the membrane with thylakoid rhodanase-like protein (TROL) and translocon on the inner envelope chloroplast membrane (Tic62), which have identical C terminal FNR binding domain [1,2]. During the electron transport, FNR anchored by TROL protein transfers electrons on NADP+ and forms NADPH which is then used in Calvin cycle as reducing agent. TROL is an integral membrane protein [3] with an inactive rhodanase-like domain (RHO) facing stroma which, as proposed earlier [4], could bind a small ligand leading to releasing or binding of FNR. FNR-TROL protein complex is necessary for optimal photosynthetic electron flow [1]. It has been shown that C4 plant maize FNR isomers have different N-terminal structure which determines binding affinity to protein complexes and different ratios of bound and unbound FNR in bundle sheath and mesophyll cells, depending on preferable photosynthetic electron transport [5]. Mutant Arabidopsis plant that contain maize FNR1 protein showed influence on dynamic association of FNR and change in excitation balance between photosystems which then influenced photo induced electron transport and finally photosynthesis [5]. In order to determine the influence of maize FNR1 on photosynthesis in C3 plants and difference in interaction strength with TROL, we preformed Yeast two hybrid screening, x-alpha-gal assay and β-galactosidase assay. Elsevier 2019-12-20 /pmc/articles/PMC6953530/ /pubmed/31938718 http://dx.doi.org/10.1016/j.dib.2019.105038 Text en © 2019 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Genetics, Genomics and Molecular Biology
Rac, Anja
Fulgosi, Hrvoje
Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title_full Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title_fullStr Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title_full_unstemmed Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title_short Qualitative and quantitative dataset of TROL protein interaction with C3 and C4 ferredoxin: NADP(+) oxidoreductases
title_sort qualitative and quantitative dataset of trol protein interaction with c3 and c4 ferredoxin: nadp(+) oxidoreductases
topic Genetics, Genomics and Molecular Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6953530/
https://www.ncbi.nlm.nih.gov/pubmed/31938718
http://dx.doi.org/10.1016/j.dib.2019.105038
work_keys_str_mv AT racanja qualitativeandquantitativedatasetoftrolproteininteractionwithc3andc4ferredoxinnadpoxidoreductases
AT fulgosihrvoje qualitativeandquantitativedatasetoftrolproteininteractionwithc3andc4ferredoxinnadpoxidoreductases