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Sökning: WFRF:(Jarvis Peter) > (2005-2009) > Monogalactosyldiacy...

LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00004855naa a2200625 4500
001oai:DiVA.org:su-58514
003SwePub
008110603s2008 | |||||||||||000 ||eng|
009oai:gup.ub.gu.se/78645
009oai:gup.ub.gu.se/195717
0247 a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-585142 URI
0247 a https://doi.org/10.1104/pp.108.1233722 DOI
0247 a https://gup.ub.gu.se/publication/786452 URI
0247 a https://gup.ub.gu.se/publication/1957172 URI
040 a (SwePub)sud (SwePub)gud (SwePub)gu
041 a engb eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Aronsson, Henrik,d 1971u Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences4 aut0 (Swepub:gu)xarohe
2451 0a Monogalactosyldiacylglycerol deficiency in Arabidopsis affects pigment composition in the prolamellar body and impairs thylakoid membrane energization and photoprotection in leaves
264 c 2008-07-18
264 1b Oxford University Press (OUP),c 2008
338 a print2 rdacarrier
500 a authorCount :7
520 a Monogalactosyldiacylglycerol (MGDG) is the major lipid constituent of chloroplast membranes and has been proposed to act directly in several important plastidic processes, particularly during photosynthesis. In this study, the effect of MGDG deficiency, as observed in the monogalactosyldiacylglycerol synthase1-1 (mgd1-1) mutant, on chloroplast protein targeting, phototransformation of pigments, and photosynthetic light reactions was analyzed. The targeting of plastid proteins into or across the envelope, or into the thylakoid membrane, was not different from wild-type in the mgd1 mutant, suggesting that the residual amount of MGDG in mgd1 was sufficient to maintain functional targeting mechanisms. In dark-grown plants, the ratio of bound protochlorophyllide (Pchlide, F656) to free Pchlide (F631) was increased in mgd1 compared to the wild type. Increased levels of the photoconvertible pigment-protein complex (F656), which is photoprotective and suppresses photooxidative damage caused by an excess of free Pchlide, may be an adaptive response to the mgd1 mutation. Leaves of mgd1 suffered from a massively impaired capacity for thermal dissipation of excess light due to an inefficient operation of the xanthophyll cycle; the mutant contained less zeaxanthin and more violaxanthin than wild type after 60 min of high-light exposure and suffered from increased photosystem II photoinhibition. This is attributable to an increased conductivity of the thylakoid membrane at high light intensities, so that the proton motive force is reduced and the thylakoid lumen is less acidic than in wild type. Thus, the pH-dependent activation of the violaxanthin de-epoxidase and of the PsbS protein is impaired.
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
650 7a NATURVETENSKAPx Biologix Botanik0 (SwePub)106072 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Botany0 (SwePub)106072 hsv//eng
653 a nadph-protochlorophyllide oxidoreductase
653 a photosynthetic electron-transport
653 a transit peptide
653 a photosystem-ii
653 a outer envelope
653 a dgd1 mutant
653 a chlorophyll fluorescence
653 a protein import
653 a inner envelope
653 a in-vivo
653 a NATURAL SCIENCES
653 a NATURVETENSKAP
7001 a Schottler, Mark A.4 aut
7001 a Kelly, Amelie A.u Stockholms universitet,Institutionen för biokemi och biofysik4 aut
7001 a Sundqvist, Christer,d 1943u Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences4 aut0 (Swepub:gu)xsunch
7001 a Dormann, Peter4 aut
7001 a Karim, Sazzad,d 1966u Gothenburg University,Göteborgs universitet,Institutionen för växt- och miljövetenskaper,Department of Plant and Environmental Sciences4 aut0 (Swepub:gu)xkasaz
7001 a Jarvis, Paul4 aut
7102 a Göteborgs universitetb Institutionen för växt- och miljövetenskaper4 org
7730 t Plant Physiologyd : Oxford University Press (OUP)g 148:1, s. 580-592q 148:1<580-592x 0032-0889x 1532-2548
8564 u http://www.plantphysiol.org/content/148/1/580.full.pdf
8564 8u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-58514
8564 8u https://doi.org/10.1104/pp.108.123372
8564 8u https://gup.ub.gu.se/publication/78645
8564 8u https://gup.ub.gu.se/publication/195717

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