State transitions, light-harvesting antenna phosphorylation and light-harvesting antenna migration in vivo in the higher plant Spirodela oligorrhiza

McCormac, Dennis J.; Bruce, Doug; Greenberg, Bruce M.

doi:10.1016/0005-2728(94)90004-3

Cited by 25 publications

(19 citation statements)

References 46 publications

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“…Phosphorylation of LHCB1 and LHCB2 polypeptides induces the migration of the outer LHCII antenna from the appressed to stroma-exposed thylakoid membrane region, thereby reducing the light-harvesting capacity of PSII (1,16,27). According to our present studies (Fig.…”

Section: Fig 4 Restoration Of the Phosphorylation Capacity Of Lhciimentioning

confidence: 81%

Phosphorylation of Light-harvesting Complex II and Photosystem II Core Proteins Shows Different Irradiance-dependent Regulation in Vivo

Rintamäki

Salonen

Suoranta

et al. 1997

Journal of Biological Chemistry

231

226

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An immunological approach using a polyclonal phosphothreonine antibody is introduced for the analysis of thylakoid protein phosphorylation in vivo. Virtually the same photosystem II (PSII) core phosphoproteins (D1, D2, CP43, and the psbH gene product) and the lightharvesting chlorophyll a/b complex II (LHCII) phosphopolypeptides (LHCB1 and LHCB2), as earlier identified by radiolabeling experiments, were recognized in both pumpkin and spinach leaves. Notably, the PSII core proteins and LHCII polypeptides were found to have a different phosphorylation pattern in vivo with respect to increasing irradiance. Phosphorylation of the PSII core proteins in leaf discs attained the saturation level at the growth light intensity, and this level was also maintained at high irradiances. Maximal phosphorylation of LHCII polypeptides only occurred at low light intensities, far below the growth irradiance, and then drastically decreased at higher irradiances. These observations are at variance with traditional studies in vitro, where LHCII shows a light-dependent increase in phosphorylation, which is maintained even at high irradiances. Only a slow restoration of the phosphorylation capacity for LHCII polypeptides at the low light conditions occurred in vivo after the high light-induced inactivation. Furthermore, if thylakoid membranes were isolated from the high light-inactivated leaves, no restoration of LHCII phosphorylation took place in vitro. However, both the high light-induced inactivation and low light-induced restoration of LHCII phosphorylation seen in vivo could be mimicked in isolated thylakoid membranes by incubating with reduced and oxidized dithiothreitol, respectively. We propose that stromal components are involved in the regulation of LHCII phosphorylation in vivo, and inhibition of LHCII phosphorylation under increasing irradiance results from reduction of the thiol groups in the LHCII kinase. Photosystem (PS)1 II is a multiprotein complex of the thyla- (14) protein phosphatases, active in dephosphorylation of thylakoid phosphoproteins, are reported to be present in plant chloroplasts. Distinct physiological roles have been established for the phosphorylation of LHCII polypeptides, being implicated in the regulation of excitation energy distribution between PSII and PSI (1, 2), and in the protection of PSII against photoinhibition (15,16). Under conditions where PSII becomes more excited than PSI, the redox-controlled kinase is activated and phosphorylates LHCII polypeptides. The outer LHCII subcomplex, consisting of LHCB1 and LHCB2 proteins (see, e.g., Ref. 17), then detaches from the PSII complex and migrates out from the appressed region of the thylakoid membrane, thereby reducing the excitation of PSII (1). Dephosphorylation of this mobile LHCII subcomplex allows its subsequent migration back to the stacked grana region and reassociation with PSII (16).The only function so far established for reversible phosphorylation of PSII core proteins is the regulation of the degradation of photodamaged D1 protein ...

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Section: Fig 4 Restoration Of the Phosphorylation Capacity Of Lhciimentioning

confidence: 81%

Phosphorylation of Light-harvesting Complex II and Photosystem II Core Proteins Shows Different Irradiance-dependent Regulation in Vivo

Rintamäki

Salonen

Suoranta

et al. 1997

Journal of Biological Chemistry

231

226

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“…Although more accurate measurements are obtainable using isolated thylakoids, it is possible to determine the F735/F685 ratio in intact leaf sections (cf. Dau & Hansin 1988; McCormac, Bruce & Greenburg 1994). To assess the antenna complex distribution in response to short‐term irradiation changes, 77 K fluorescence measurements were made on leaves after incubation as described above.…”

Section: Resultsmentioning

confidence: 99%

Rapid, reversible alterations in spinach thylakoid appression upon changes in light intensity

Rozak¹,

Seiser

Wacholtz

et al. 2002

Plant Cell & Environment

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“…Since the stromal protein phosphatase is able to dephosphorylate thylakoid proteins that are membrane-bound, the enzyme has the potential to be involved in the reversible phosphorylation of LHC-11. It is presumed that as the LHC-11, situated with PSII in the granal thylakoids, becomes phosphorylated it migrates to the granal margins or to nonappressed stromal thylakoids (Bennett, 1991;McCormack et al, 1994;Allen, 1995). This migration is concomitant with the state 1 to state 2 transition, which regulates quanta1 energy distribution of the two photosystems.…”

Section: Discussionmentioning

confidence: 99%

Purification of a Protein Phosphatase from Chloroplast Stroma Capable of Dephosphorylating the Light-Harvesting Complex-II

1997

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A protein phosphatase was purified from the stroma of Pea (Pisum sativum L.) chloroplasts that is capable of dephosphorylating synthetic phosphopeptides. Following chromatographic purification of greater than 400-fold, two-dimensional electrophoresis indicated that the stromal protein phosphatase is a 29-kD protein. A similar molecular size was determined for the protein-phosphatase activity using gel-permeation chromatography, indicating that the stromal protein phosphatase is probably a monomer. The purified enzyme was able to dephosphorylate synthetic phosphopeptides, which mimic the thylakoid light-harvesting complex-ll (LHC-II) N terminus, as well as LHC-II in thylakoid membranes, but did not dephosphorylate the major 64-kD phosphoprotein in the stroma. The stromal protein phosphatase did not discriminate between dephosphorylation of phosphothreonine and phosphoserine residues in synthetic peptide substrates, providing further evidence that this enzyme is distinct from the protein phosphatase localized in thylakoid membranes. The exact physiological role of the stromal protein phosphatase has yet to be determined, but it may function in the dephosphorylation of LHC-II.

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State transitions, light-harvesting antenna phosphorylation and light-harvesting antenna migration in vivo in the higher plant Spirodela oligorrhiza

Cited by 25 publications

References 46 publications

Phosphorylation of Light-harvesting Complex II and Photosystem II Core Proteins Shows Different Irradiance-dependent Regulation in Vivo

Phosphorylation of Light-harvesting Complex II and Photosystem II Core Proteins Shows Different Irradiance-dependent Regulation in Vivo

Rapid, reversible alterations in spinach thylakoid appression upon changes in light intensity

Purification of a Protein Phosphatase from Chloroplast Stroma Capable of Dephosphorylating the Light-Harvesting Complex-II

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