The light‐dependent accumulation of the P700 chlorophyll <i>a</i> protein of the photosystem I reaction center in barley

Kreuz, Klaus; Dehesh, Katayoon; Apel, Klaus

doi:10.1111/j.1432-1033.1986.tb09908.x

Cited by 67 publications

(25 citation statements)

References 54 publications

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“…In contrast, the appearance of the chlorophyllbinding proteins of the reaction centers of PSI and PSII is dependent on illumination (Fig. 4, Kreuz et al 1986;Sutton et al 1987;Schrubar et al 1991). Thus, although the concentration of NDH-H increases during illumination, the expression is not coordinated with the synthesis of proteins for the photosynthetic apparatus.…”

Section: Discussionmentioning

confidence: 99%

Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Berger

Ellersiek

Westhoff

et al. 1993

Planta

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Abstract. The plastid genomes of higher plants contain eleven reading frames (ndhA-K) that are homologous to genes encoding subunits of the mitochondrial NADHubiquinone-oxidoreductase (complex I). The carboxyterminal end of the NDH-H subunit from rice (Oryza sativa L.) was expressed as a fusion protein in Escherichia coli and antibodies against the fusion protein were generated in rabbits. The antibody was used to study the expression of NDH-H, and the following results were obtained: (i) NDH-H is expressed in mono-and dicotyledonous plants, (ii) NDH-H is localized on the stroma lamellae of the thylakoid membrane and (iii) NDH-H is expressed in etioplasts. Together with the finding that two other ndh genes (ndhI and ndhK) are expressed in plastids, these results point to the existence of an NAD(P)H-plastoquinone-oxidoreductase on the thylakoid membrane. The possible function of the enzyme in plastids is discussed and it is suggested that it works in balancing the ATP/ADP and the NADPH/NADP ratios during changing external (i.e. light) or internal (i.e. ATP and NADPH demands of biosynthetic pathways of the plastid) conditions.

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Section: Discussionmentioning

confidence: 99%

Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Berger

Ellersiek

Westhoff

et al. 1993

Planta

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“…Since mRNAs coding for these apoproteins are present already in etiolated plants (Herrmann et al, 1985;Klein and Mullet, 1986;Kreuz et al, 1986), Chl synthesis must interact with some post-transcriptional process but the step of interaction remained unknown. In the present study, we tested interaction of Chl with proteolysis of apoproteins and with initiation of translation.…”

Section: Discussionmentioning

confidence: 99%

“…Etioplasts do not synthesize chlorophyll nor do they accumulate nuclear-encoded chlorophyll-u/h-binding apoproteins (Apel, 1979;Bennett, 1981;Bennett et al, 1984) or plastid-encoded chlorophyll a binding apoproteins (Herrmann et al, 1985;Klein and Mullet, 1986;Kreuz et al, 1986;Sutton et al, 1987;Gamble et al, 1989) although they accumulate protochlorophyllide, a chlorophyll precursor. When plants are illuminated, protochlorophyllide (PChlide) is reduced to chlorophyllide (Chlide) by protochlorophyllide reductase (Apel et al, 1980) in a reaction dependent on light and NADPH.…”

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confidence: 99%

Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts

Eichacker

Paulsen

Rüdiger

1992

European Journal of Biochemistry

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Accumulation of plastid-encoded chlorophyll apoproteins and chlorophyll synthesis are controlled by light in angiosperms. An in vitro system utilizing isolated and lysed barley (Hordeum vulgare L.) etioplasts revealed the specific accumulation of P700, CP47, CP43 and D2 triggered by de nova synthesis of chlorophyll. Accumulation rates of radiolabelled chlorophyll apoproteins were linear for about 30 min. Pulse/chase translation assays showed that synthesis of chlorophyll does not result in increased chlorophyll apoprotein stability. Instead turnover rates of chlorophyll apoproteins were higher in the presence than in the absence of chlorophyll. Chlorophyll-dependent accumulation of chlorophyll apoproteins must therefore be regulated on the level of translation. Translation of chlorophyll apoproteins was blocked to about 50% by addition of 30-50 pM aurintricarboxylic acid or 20 pM kasugamycin. The kinetics of chlorophyll-dependent translation indicated that the in vitro translation system is capable of translation initiation. The capability of translation initiation was lost in lysed etioplasts after preincubation for at least 5 min without chlorophyll synthesis. The results suggest that initiation is involved in chlorophyll-dependent regulation of translation.The development of photosynthetically active plastids from proplastids requires activation of a large number of nuclear and plastid genes. A central question, therefore, concerns the nature and origin of signals that initiate and control this process. A key requirement in the control of developmental processes in higher plants is fulfilled by light which acts as environmental control factor regulating the accumulation of some nuclear genes for plastid-localized proteins on such diverse levels as transcription (Fluhr et al., 1986), translation (Slovin and Tobin, 1982) and protein stability (Bennett, 1981).

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“…For example, transcripts from all nuclear genes studied accumulate with comparable kinetics when spinach seedlings are transferred from darkness to light, while the corresponding proteins display pronounced differences: some of them, for instance, the ATP synthase subunits y and 6, the Rieske Fe/S protein of the cytochrome complex, the peripheral polypeptides plastocyanin, ferredoxin-NADP'-oxidoreductase, and the extrinsic polypeptides of the oxygen-evolving system are synthesized effectively from minute RNA amounts in the dark and accumulate only moderately during greening. Others, such as all chlorophyllbinding proteins of both nuclear (Apel, 1979;Bennett, 1981 ; Bennett et a]., 1984) and plastid (Herrmann et al, 1985(Herrmann et al, , 1992Klein and Mullet, 1986;Kreuz et al, 1986;Sutton et al, 1987;Gamble et al, 1989) origin fail to accumulate in the dark, although the corresponding mRNAs can be detected as well.…”

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confidence: 99%

Post‐transcriptional and post‐translational regulatory steps are crucial in controlling the appearance and stability of thylakoid polypeptides during the transition of etiolated tobacco seedlings to white light

Palomares

Herrmann

Oelmüller

1993

European Journal of Biochemistry

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We have investigated the expression of nuclear-encoded chloroplast proteins that are not associated with chlorophyll (the lumenal 33-kDa and 23-kDa polypeptides of the oxygen-evolving system of photosystem 11, plastocyanin and the Rieske Fe/S protein) by comparing mRNA-accumulation rates with those of the corresponding proteins during illumination of etiolated tobacco seedlings. Using subcellular fractionation, pulsekhase, Northern and Western techniques, we found that the biogenesis and stability of these proteins are regulated both translationally, as well as post-translationally, including the efficiency of mRNA uptake into polysomes, processes that operate between translation and assembly or monitor the status (soluble and membrane-attached) of a terminally processed polypeptide. Polypeptide synthesis is generally not limited by mRNA amounts. For instance, steady-state transcript levels may increase 10-fold during illumination, while those associated with polycomes increase only 2-3-fold without measurable influence on the rate of protein synthesis. The 23-kDa and Rieske polypeptides are predominantely membrane associated, but plastocyanin and the 33-kDa polypeptide are distributed among both soluble and membrane-associated protein fractions. Plastocyanin appears to be comparably stable in both forms. However, for the 33-kDa polypcptide, only the membrane-attached form is stable (> 8 h) and only this pool increases upon illumination. Its soluble form is rapidly degraded with a half-life of approximately 1 h under the chosen conditions. Our findings probably reflect part of a more general regulatory principle operating in the differentiation and maintenance of subcellular structure.Thylakoid membranes of higher plants consist of approximately 70 polypcptide species, the majority of which are assembled in five major multisubunit complexes, the photosystems I and 11, the cytochrome complex, the ATP synthase and the NAD(P)H dehydrogenase. Most of the genes that code for these polypeptides have been isolated during the past decadc (summarized in Hallick, 1989, andHemnann et al., 1991); approximately half of them originate in plastids, the remaining in the nucleus. The dual genetic origin and a vast difference of 2-3 orders of magnitude in genc-copy number between nucleus and plastids implies that the synthcsis and assembly of thylakoid polypeptides must be highly coordinated in time and space, with regard to stoichiometry, and in response to external stimuli.Light plays a crucial role among the various factors that influence the biosynthesis of the photosynthetic membranc and appears to operate at various levels. The light-dependent synthesis of polypeptides made in plastids is generally controlled post-transcriptionally (Herrmann et al

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The light‐dependent accumulation of the P700 chlorophyll a protein of the photosystem I reaction center in barley

Cited by 67 publications

References 54 publications

Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Studies on the expression of NDH-H, a subunit of the NAD(P)H-plastoquinone-oxidoreductase of higher-plant chloroplasts

Synthesis of chlorophyll a regulates translation of chlorophyll a apoproteins P700, CP47, CP43 and D2 in barley etioplasts

Post‐transcriptional and post‐translational regulatory steps are crucial in controlling the appearance and stability of thylakoid polypeptides during the transition of etiolated tobacco seedlings to white light

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