N-Terminal Structure of Maize Ferredoxin:NADP(+) Reductase Determines Recruitment into Different Thylakoid Membrane Complexes

DC FieldValueLanguage
dc.contributor.authorTwachtmann, Manuel
dc.contributor.authorAltmann, Bianca
dc.contributor.authorMuraki, Norifumi
dc.contributor.authorVoss, Ingo
dc.contributor.authorOkutani, Satoshi
dc.contributor.authorKurisu, Genji
dc.contributor.authorHase, Toshiharu
dc.contributor.authorHanke, Guy T.
dc.date.accessioned2021-12-23T16:11:36Z-
dc.date.available2021-12-23T16:11:36Z-
dc.date.issued2012
dc.identifier.issn10404651
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/9786-
dc.description.abstractTo adapt to different light intensities, photosynthetic organisms manipulate the flow of electrons through several alternative pathways at the thylakoid membrane. The enzyme ferredoxin:NADP(+) reductase (FNR) has the potential to regulate this electron partitioning because it is integral to most of these electron cascades and can associate with several different membrane complexes. However, the factors controlling relative localization of FNR to different membrane complexes have not yet been established. Maize (Zea mays) contains three chloroplast FNR proteins with totally different membrane association, and we found that these proteins have variable distribution between cells conducting predominantly cyclic electron transport (bundle sheath) and linear electron transport (mesophyll). Here, the crystal structures of all three enzymes were solved, revealing major structural differences at the N-terminal domain and dimer interface. Expression in Arabidopsis thaliana of maize FNRs as chimeras and truncated proteins showed the N-terminal determines recruitment of FNR to different membrane complexes. In addition, the different maize FNR proteins localized to different thylakoid membrane complexes on expression in Arabidopsis, and analysis of chlorophyll fluorescence and photosystem I absorbance demonstrates the impact of FNR location on photosynthetic electron flow.
dc.description.sponsorshipMonbu KagakushoMinistry of Education, Culture, Sports, Science and Technology, Japan (MEXT) [18770035]; Deutsche Forschungsgemeinshaft Grant within Sonderforschungsbereich [P2]; The financial support of the Monbu Kagakusho Grant-in-Aid for Young Scientists 18770035 and the Deutsche Forschungsgemeinshaft Grant P2 within Sonderforschungsbereich 944 is gratefully acknowledged. We thank Renate Scheibe for helpful discussion.
dc.language.isoen
dc.publisherAMER SOC PLANT BIOLOGISTS
dc.relation.ispartofPLANT CELL
dc.subjectBiochemistry & Molecular Biology
dc.subjectBUNDLE-SHEATH
dc.subjectCell Biology
dc.subjectCHLOROPHYLL-A FLUORESCENCE
dc.subjectCYCLIC ELECTRON FLOW
dc.subjectCYTOCHROME B(6)F COMPLEX
dc.subjectDEHYDROGENASE COMPLEX
dc.subjectFERREDOXIN-NADP(+) REDUCTASE
dc.subjectNADP+ OXIDOREDUCTASE
dc.subjectPHOTOSYSTEM-I
dc.subjectPlant Sciences
dc.subjectQUANTUM YIELD
dc.subjectREDOX POISE
dc.titleN-Terminal Structure of Maize Ferredoxin:NADP(+) Reductase Determines Recruitment into Different Thylakoid Membrane Complexes
dc.typejournal article
dc.identifier.doi10.1105/tpc.111.094532
dc.identifier.isiISI:000308352800022
dc.description.volume24
dc.description.issue7
dc.description.startpage2979
dc.description.endpage2991
dc.contributor.orcid0000-0002-5354-0807
dc.contributor.orcid0000-0003-4112-2955
dc.contributor.researcheridH-9271-2013
dc.contributor.researcheridABA-5960-2020
dc.contributor.researcheridAAW-2540-2020
dc.publisher.place15501 MONONA DRIVE, ROCKVILLE, MD 20855 USA
dcterms.isPartOf.abbreviationPlant Cell
dcterms.oaStatusGreen Published, Bronze
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidHaGu059-
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