title: Structural organization of photosynthetic apparatus in agranal chloroplasts of maize.
abstract: We investigated the organization of photosystem II (PSII) in agranal bundle sheath thylakoids from a C(4) plant maize. Using blue native/SDS-PAGE and single particle analysis, we show for the first time that PSII in the bundle sheath (BS) chloroplasts exists in a dimeric form and forms light-harvesting complex II (LHCII).PSII supercomplexes. We also demonstrate that a similar set of photosynthetic membrane complexes exists in mesophyll and agranal BS chloroplasts, including intact LHCI.PSI supercomplexes, PSI monomers, PSII core dimers, PSII monomers devoid of CP43, LHCII trimers, LHCII monomers, ATP synthase, and cytochrome b(6)f complex. Fluorescence functional measurements clearly indicate that BS chloroplasts contain PSII complexes that are capable of performing charge separation and are efficiently sensitized by the associated LHCII. We identified a fraction of LHCII present within BS thylakoids that is weakly energetically coupled to the PSII reaction center; however, the majority of BS LHCII is shown to be tightly connected to PSII. Overall, we demonstrate that organization of the photosynthetic apparatus in BS agranal chloroplasts of a model C(4) plant is clearly distinct from that of the stroma lamellae of the C(3) plants. In particular, supramolecular organization of the dimeric LHCII.PSII in the BS thylakoids strongly suggests that PSII in the BS agranal membranes may donate electrons to PSI. We propose that the residual PSII activity may supply electrons to poise cyclic electron flow around PSI and prevent PSI overoxidation, which is essential for the CO(2) fixation in BS cells, and hence, may optimize ATP production within this compartment.
authors.affiliation: Department of Plant Physiology, University of Warsaw, Miecznikowa 1, 02-096 Warsaw, Poland. romanela@biol.uw.edu.pl
authors.forename: Elzbieta
authors.initials: E
authors.lastname: Romanowska
authors.forename: Joanna
authors.initials: J
authors.lastname: Kargul
authors.forename: Marta
authors.initials: M
authors.lastname: Powikrowska
authors.forename: Giovanni
authors.initials: G
authors.lastname: Finazzi
authors.forename: Jon
authors.initials: J
authors.lastname: Nield
authors.forename: Anna
authors.initials: A
authors.lastname: Drozak
authors.forename: Berenika
authors.initials: B
authors.lastname: Pokorska
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry; D002245:Carbon Dioxide / Q000737:chemistry; D002736:Chloroplasts / Q000378:metabolism*; D045346:Cytochrome b6f Complex / Q000737:chemistry; D004583:Electrons; D045342:Light-Harvesting Protein Complexes / Q000737:chemistry; D025261:Mitochondrial Proton-Translocating ATPases / Q000378:metabolism; D008954:Models, Biological; D009249:NADP / Q000737:chemistry; D010788:Photosynthesis; D045322:Photosynthetic Reaction Center Complex Proteins / Q000737:chemistry; D045332:Photosystem II Protein Complex / Q000378:metabolism; D013050:Spectrometry, Fluorescence / Q000379:methods; D020524:Thylakoids / Q000378:metabolism; D003313:Zea mays / Q000235:genetics* / Q000378:metabolism*
chemical_list: D045342:Light-Harvesting Protein Complexes; D045322:Photosynthetic Reaction Center Complex Proteins; D045332:Photosystem II Protein Complex; D002245:Carbon Dioxide; D009249:NADP; D000255:Adenosine Triphosphate; D045346:Cytochrome b6f Complex; D025261:Mitochondrial Proton-Translocating ATPases