Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll <i>a</i>-Apoproteins Requires Chlorophyll <i>a</i>

Klein, Robert R.; Gamble, Patricia E.; Mullet, John E.

doi:10.1104/pp.88.4.1246

Cited by 61 publications

(51 citation statements)

References 33 publications

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“…In contrast, elongation and accumulation of the D2 protein were nearly unaffected by light, in agreement with earlier observations in etioplasts [28]. Thus translation elongation and accumulation of the D2 protein might be independent of de novo chlorophyll biosynthesis.…”

Section: Discussionsupporting

confidence: 79%

Light is required for efficient translation elongation and subsequent integration of the D1‐protein into Photosystem II

Wijk

Eichacker²

1996

FEBS Letters

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The light dependence of translation and successive assembly of the D1 reaction center protein into Photosystem II subcomplexes was followed in fully developed chloroplasts isolated from the dark phase of diurnally grown spinach. The incorporation of synthesized D1 protein into Photosystem II (PSII) was analyzed by fractionation of radiolabeled unassembled protein and PSII (sub)complexes on sucrose density gradients. The ribosomes with attached nascent chains were recovered as pellets in the same gradients, and nascent chains of the D1 protein were immunoprccipitated. The analysis showed that absence of light during translation leads to an increased accumulation of polysome-bound D1 translation intermediates, indicating that light is required for efficient elongation of the D1 protein. The accumulation of the D1 protein and CP43 decreased three-fold in darkness, whereas accumulation of the D2 reaction center protein was not affected by light. In addition, light was also required for efficient incorporation of the D1 protein into the PSII core complex. In darkness, the newly synthesized D1 protein accumulated predominantly as unassembled protein or in PSII subcomplexes smaller than 100 kDa.

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Section: Discussionsupporting

confidence: 79%

Light is required for efficient translation elongation and subsequent integration of the D1‐protein into Photosystem II

Wijk

Eichacker²

1996

FEBS Letters

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“…In particular, light-induced Chl biosynthesis triggers the accumulation of the chloroplast-encoded Chl proteins (Klein et al, 1988a;Eichacker et al, 1992). Chl does not alter Chl apoprotein mRNA level or the distribution of mRNA in polysomes, indicating that Chl activates Chl protein accumulation posttranscriptionally (Klein et al, 1988b).…”

Section: Discussionmentioning

confidence: 99%

Chlorophyll Regulates Accumulation of the Plastid-Encoded Chlorophyll Proteins P700 and D1 by Increasing Apoprotein Stability

Kim¹,

Eichacker²,

Rüdiger³

et al. 1994

Plant Physiol.

140

103

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Chlorophyll protein accumulation in barley (Hordeum vulgare 1.) chloroplasts is controlled posttranscriptionally by light-induced formation of chlorophyll a. l h e abundance of translation initiation complexes associated with psbA, psaA, and rbcL mRNAs was measured using extension and inhibition analysis in plants grown in the dark for 4.5 d and then illuminated for up to 16 h. Light-induced accumulation of the chlorophyll proteins was not accompanied by changes in the abundance of translation initiation complexes, indicating that regulation of chlorophyll protein accumulation at this stage of development does not occur at the level of translation initiation. Translational runoff assays were performed in the presente of lincomycin, an inhibitor of translation initiation, to determine whether chlorophyll protein accumulation was regulated at the level of translation elongation. l h e extent of ribosome runoff of psaA and psbA mRNAs was similar in the presence or absence of chlorophyll, indicating that chlorophyll did not alter chlorophyll protein translation elongation. Polysome-associated D1 translation intermediates were radiolabeled in the presence or absence of chlorophyll, even though full-length D1 accumulated only in the presence of chlorophyll. Chlorophyll influenced the stability of D 1 translation intermediates to a small extent and greatly increased D 1 stability after release from ribosomes. Overall, these results demonstrate that light-induced chlorophyll biosynthesis triggers the accumulation of the chlorophyll proteins D1 and P700 in barley chloroplasts by enhancement of chlorophyll apoprotein stability.

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“…All manipulations of seedlings before light treatments were conducted in complete darkness or with light provided by a dim green safelight as described previously (10).…”

Section: Plant Growth and Mutant Identificationmentioning

confidence: 99%

“…Barley (Hordellm vulgare L. var Morex) seedlings were planted and grown as described previously (10,13). Seedlings were grown and maintained in a dark chamber in a light-tight room.…”

Section: Plant Growth and Mutant Identificationmentioning

confidence: 99%

Regulation of Light-Induced Chloroplast Transcription and Translation in Eight-Day-Old Dark-Grown Barley Seedlings

Klein¹

1991

Plant Physiol.

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Plastid transcription and translation are light-activated in 8-day-old dark-grown barley (Hordeum vulgare L.) seedlings. Pretreatment of dark-grown seedlings with cycloheximide (inhibitor of cytoplasmic protein synthesis) abolished the activation of rbcL, psbA, and psaA-B transcription by light. In contrast, inhibition of plastid protein synthesis by chloramphenicol stimulated lightactivated transcription of rbcL, psbA, and psaA-B. Light-induced transcription of the plastid genome occurred normally in the chlorophyll-deficient mutant xan-J". These results suggest that although the light-induced activation of plastid transcription is modulated by cytoplasmic and organellar protein synthesis, transcriptional activation is not dependent on the absorption of light by protochlorophyllide or the attainment of photosynthetic competence. In addition, plastid translation increased dramatically when 8-day-old dark-grown seedlings were illuminated and activation was dependent on cytoplasmic protein synthesis. Blockage of light-activated plastid transcription by Tagetin treatment (inhibitor of plastid RNA polymerase) did not attenuate the activation of plastid translation by light. These results suggest that while light simultaneously activates plastid transcription and translation, the rapid burst in plastid protein synthesis is due mainly to cytoplasmic-denved changes that regulate the rate of translation of pre-existing mRNAs.

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Light-Dependent Accumulation of Radiolabeled Plastid-Encoded Chlorophyll a-Apoproteins Requires Chlorophyll a

Abstract: The accumulation of radiolabeled plastid-encoded chlorophyll a-apoproteins is light dependent and is controlled at a posttranscriptional level.

Cited by 61 publications

References 33 publications

Light is required for efficient translation elongation and subsequent integration of the D1‐protein into Photosystem II

Light is required for efficient translation elongation and subsequent integration of the D1‐protein into Photosystem II

Chlorophyll Regulates Accumulation of the Plastid-Encoded Chlorophyll Proteins P700 and D1 by Increasing Apoprotein Stability

Regulation of Light-Induced Chloroplast Transcription and Translation in Eight-Day-Old Dark-Grown Barley Seedlings

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