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At least 19 recordsLinked to original sources
PubMed1996

Conversion of chlorophyll b to chlorophyll a via 7-hydroxymethyl chlorophyll.

Chlorophyll b is synthesized from chlorophyll a by the oxidation of the methyl group on the ring B of the tetrapyrrole ring to the formyl group. Previously, we reported that chlorophyllide b could be converted to chlorophyll a in isolated cucumber etioplasts indicating the conversion of chlorophyll b to chlorophyll a. To identify the intermediate molecule, we used barley etioplasts instead of cucumber. Chlorophyll a and an additional pigment were found after incubation of chlorophyllide b with isolated barley etioplasts. The pigment has the same retention time and absorption spectrum as 7-hydroxymethyl chlorophyll, which has the hydroxymethyl group on ring B instead of the formyl group of chlorophyll b. Authentic 7-hydroxymethyl chlorophyll was prepared by reduction of chlorophyll b by NaBH4. Chlorophyll a accumulated during the incubation of 7-hydroxymethyl chlorophyllide with etioplasts. These findings indicate that chlorophyll b is converted to chlorophyll a via 7-hydroxymethyl chlorophyll. Chlorophyll b and 7-hydroxymethyl chlorophyll accumulated within a short period of incubation of chlorophyllide b with etioplasts. However, chlorophyll a accumulated with a concomitant decrease of chlorophyll b and 7-hydroxymethyl chlorophyll. These observations also suggest that chlorophyll b is converted to 7-hydroxymethyl chlorophyll and then to chlorophyll a. Both steps required ATP.

Carbon Radioisotopes↗
PubMed1997

Conversion of Chlorophyll b to Chlorophyll a and the Assembly of Chlorophyll with Apoproteins by Isolated Chloroplasts.

The photosynthetic apparatus is reorganized during acclimation to various light environments. During adaptation of plants grown under a low-light to high-light environment, the light-harvesting chlorophyll a/b-protein complexes decompose concomitantly with an increase in the core complex of photosystem II. To study the mechanisms for reorganization of photosystems, the assembly of chlorophyll with apoproteins was investigated using isolated chloroplasts. When [14C]chlorophyllide b was incubated with chloroplasts in the presence of phytyl pyrophosphate, it was esterified and some of the [14C]chlorophyll b was converted to [14C]chlorophyll a via 7-hydroxymethyl chlorophyll. [14C]Chlorophyll a and b were incorporated into chlorophyll-protein complexes. Light-harvesting chlorophyll a/b-protein complexes of PSII had a lower [14C]chlorophyll a to [14C]chlorophyll b ratio than P700-chlorophyll a-protein complexes, indicating the specific binding of chlorophyll to apoproteins in our systems. 7-Hydroxymethyl chlorophyll, an intermediate molecule from chlorophyll b to chlorophyll a, did not become assembled with any apoproteins. These results indicate that chlorophyll b is released from light-harvesting chlorophyll a/b-protein complexes of photosystem II and converted to chlorophyll a via 7-hydroxymethyl chlorophyll in the lipid bilayer and is then used for the formation of core complexes of photosystems. These mechanisms provide the fast, fine regulation of the photosynthetic apparatus during construction of photosystems.

Journal Article↗
PubMed2001

Effects of chlorophyll a, chlorophyll b, and xanthophylls on the in vitro assembly kinetics of the major light-harvesting chlorophyll a/b complex, LHCIIb.

The major light-harvesting chlorophyll a/b complex (LHCIIb) of photosystem II in higher plants can be reconstituted with pigments in lipid-detergent micelles. The pigment-protein complexes formed are functional in that they perform efficient internal energy transfer from chlorophyll b to chlorophyll a. LHCIIb formation in vitro, can be monitored by the appearance of energy transfer from chlorophyll b to chlorophyll a in time-resolved fluorescence measurements. LHCIIb is found to form in two apparent kinetic steps with time constants of about 30 and 200 seconds. Here we report on the dependence of the LHCIIb formation kinetics on the composition of the pigment mixture used in the reconstitution. Both kinetic steps slow down when the concentration of either chlorophylls or carotenoids is reduced. This suggests that the slower 200 seconds formation of functional LHCIIb still includes binding of both chlorophylls and carotenoids. LHCIIb formation is accelerated when the chlorophylls in the reconstitution mixture consist predominantly of chlorophyll a although the complexes formed are thermally less stable than those reconstituted with a chlorophyll a:b ratio < or = 1. This indicates that although chlorophyll a binding is more dominant in the observed rate of LHCIIb formation, the occupation of (some) chlorophyll binding sites with chlorophyll b is essential for complex stability. The accelerating effect of various carotenoids (lutein, zeaxanthin, violaxanthin, neoxanthin) on LHCIIb formation correlates with their affinity to two lutein-specific binding sites. We conclude that the occupation of these two carotenoid binding sites but not of the third (neoxanthin-specific) binding site is an essential step in the assembly of LHCIIb in vitro.

Binding Sites↗
PubMed1998

Chlorophyll a oxygenase (CAO) is involved in chlorophyll b formation from chlorophyll a.

Chlorophyll b is an ubiquitous accessory pigment in land plants, green algae, and prochlorophytes. Its biosynthesis plays a key role in the adaptation to various light environments. We isolated six chlorophyll b-less mutants by insertional mutagenesis by using the nitrate reductase or argininosuccinate lyase genes as tags and examined the rearrangement of mutant genomes. We found that an overlapping region of a nuclear genome was deleted in all mutants and that this encodes a protein whose sequence is similar to those of methyl monooxygenases. This coding sequence also contains putative binding domains for a [2Fe-2S] Rieske center and for a mononuclear iron. The results demonstrate that a chlorophyll a oxygenase is involved in chlorophyll b formation. The reaction mechanism of chlorophyll b formation is discussed.

Amino Acid Sequence↗
PubMed1994

Ultrafast chlorophyll b-chlorophyll a excitation energy transfer in the isolated light harvesting complex, LHC II, of green plants. Implications for the organisation of chlorophylls.

The excitation energy transfer between chlorophyll b (Chl b) and chlorophyll a (Chl a) in the isolated trimeric chlorophyll-a/b-binding protein complex of spinach photosystem 2 (LHC II) has been studied by femtosecond spectroscopy. In the main absorption band of Chl b the ground state recovery consists of two components of 0.5 ps and 2.0 ps, respectively. Also in the Chl a absorption band, at 665 nm, the ground state recovery is essentially bi-exponential. In this case is, however, the fastest relaxation lifetime is a 2.0 ps component followed by a slower component with a lifetime in the order of 10-20 ps. In the Chl b absorption band a more or less constant anisotropy of r = 0.2 was observed during the 3 ps the system was monitored. In the Chl a absorption band there was, however, a relaxation of the anisotropy from r = 0.3 to a quasi steady state level of r = 0.18 in about 1 ps. Since the 0.5 ps component is only seen upon selective excitation of Chl b we assign this component to the energy transfer between Chl b and Chl a. The other components most likely represents redistribution processes of energy among spectrally different forms of Chl a. The energy transfer process between Chl b and Chl a can well be explained by the Förster mechanism which also gives a calculated distance of 13 A between interacting chromophores. The organisation of chlorophylls in LHC II is discussed in view of the recent crystal structure data (1991) Nature 350, 130].

Chlorophyll↗
PubMed1999

Chlorophyll b to chlorophyll a conversion precedes chlorophyll degradation in Hordeum vulgare L.

This study reveals by in vivo deuterium labeling that in higher plants chlorophyll (Chl) b is converted to Chl a before degradation. For this purpose, de-greening of excised green primary leaves of barley (Hordeum vulgare) was induced by permanent darkness in the presence of heavy water (80 atom % (2)H). The resulting Chl a catabolite in the plant extract was subjected to chemical degradation by chromic acid. 3-(2-Hydroxyethyl)-4-methyl-maleimide, the key fragment that originates from the Chl catabolite, was isolated. High resolution (1)H-, (2)H-NMR and mass spectroscopy unequivocally demonstrates that a fraction of this maleimide fragment consists of a mono-deuterated methyl group. These results suggest that Chl b is converted into Chl a before degradation. Quantification proves that the initial ratio of Chl a:Chl b in the green plant is preserved to about 60-70% in the catabolite composition isolated from yellowing leaves. The incorporation of only one deuterium atom indicates the involvement of two distinguishable redox enzymes during the conversion.

Chlorophyll↗
PubMed2002

Determination of relative chlorophyll binding affinities in the major light-harvesting chlorophyll a/b complex.

The major light-harvesting complex (LHCIIb) of photosystem II can be reconstituted in vitro from its recombinant apoprotein in the presence of a mixture of carotenoids and chlorophylls a and b. By varying the chlorophyll a/b ratio in the reconstitution mixture, the relative amounts of chlorophyll a and chlorophyll b bound to LHCIIb can be changed. We have analyzed the chlorophyll stoichiometry in recombinant wild type and mutant LHCIIb reconstituted at different chlorophyll a/b ratios in order to assess relative affinities of the chlorophyll-binding sites. This approach reveals five sites that exclusively bind chlorophyll b. Another site exhibits a slight preference of chlorophyll b over chlorophyll a. The remaining six sites are filled preferentially with chlorophyll a but also tolerate chlorophyll b when this is offered at a large excess. Three of these chlorophyll a-affine sites could be assigned to distinct positions defined by the three-dimensional LHCIIb structure. Exclusive chlorophyll b sites complemented by chlorophyll a sites that are selective only to a certain extent are consistent with the observation that chlorophyll b but not chlorophyll a is essential for reconstituting stable LHCIIb. These data offer an explanation why a rather constant chlorophyll a/b ratio is observed in native LHCIIb despite the apparent promiscuity of some binding sites.

Amino Acid Substitution↗
PubMed1978

Analyses of absorption and fluorescence spectra of water-soluble chlorophyll proteins, pigment system II particles and chlorophyll a in diethylether solution by the curve-fitting method.

Absorption and fluorescence spectra in the red region of water-soluble chlorophyll proteins, Lepidium CP661, CP663 and Brassica CP673, pigment System II particles of spinach chloroplasts and chlorophyll a in diethylether solution at 25 degrees C were analyzed by the curve-fitting method (French, C.S., Brown, J.S. and Lawrence, M.C. (1972) Plant Physiol 49, 421--429). It was found that each of the chlorophyll forms of the chlorophyll proteins and the pigment System II particles had a corresponding fluorescence band with the Stokes shift ranging from 0.6 to 4.0 nm. The absorption spectrum of chlorophyll a in diethylether solution was analyzed to one major band with a peak at 660.5 nm and some minor bands, while the fluorescence spectrum was analyzed to one major band with a peak at 664.9 nm and some minor bands. A mirror image was clearly demonstrated between the resolved spectra of absorption and fluorescence. The absorption spectrum of Lepidium CP661 was composed of a chlorophyll b form with a peak at 652.8 nm and two chlorophyll a forms with peaks at 662.6 and 671.9 nm. The fluorescence spectrum was analyzed to five component bands. Three of them with peaks at 654.8, 664.6 and 674.6 nm were attributed to emissions of the three chlorophyll forms with the Stokes shift of 2.0--2.7 nm. The absorption spectrum of Brassica CP673 had a chlorophyll b form with a peak at 653.7 nm and four chlorophyll a forms with peaks at 662.7, 671.3, 676.9 and 684.2 nm. The fluorescence spectrum was resolved into seven component bands. Four of them with peaks at 666.7, 673.1, 677.5 and 686.2 nm corresponded to the four chlorophyll a forms with the Stokes shift of 0.6--4.0 nm. The absorption spectrum of the pigment System II particles had a chlorophyll b form with a peak at 652.4 nm and three chlorophyll a forms with peaks at 662.9, 672.1 and 681.6 nm. The fluorescence spectrum was analyzed to four major component bands with peaks at 674.1, 682.8, 692.0 and 706.7 nm and some minor bands. The former two bands corresponded to the chlorophyll a forms with peaks at 672.1 and 681.6 nm with the Stokes shift of 2.0 and 1.2 nm, respectively. Absorption spectra at 25 degrees C and at --196 degrees C of the water-soluble chlorophyll proteins were compared by the curve-fitting methods. The component bands at --196 degrees C were blue-shifted by 0.8--4.1 nm and narrower in half widths as compared to those at 25 degrees C.

Chlorophyll↗
PubMed1997

Analysis of some optical properties of a native and reconstituted photosystem II antenna complex, CP29: pigment binding sites can be occupied by chlorophyll a or chlorophyll b and determine spectral forms.

The minor photosystem II antenna complex CP29(Lhcb-4) has been reconstituted in vitro with the Lhcb-4 apoprotein, overexpressed in Escherichia coli, and the native pigments. Modulation of the pigment composition during reconstitution yields binding products with markedly different chlorophyll a/b binding ratios even though the total number of bound chlorophylls (a plus b) remains constant at eight. A thermodynamic analysis of steady state absorption and fluorescence spectra demonstrates that all chlorophylls are energetically coupled, while the kinetics of chlorophyll photooxidation indicate that triplet chlorophyll-carotenoid coupling is also conserved during pigment binding in vitro. The influence of the chlorophyll a/b binding ratio on the absorption spectra measured at 72 and 300 K is analyzed for the Qy absorption region. Increased chlorophyll b binding leads to large increases in absorption in the 640-660 nm region, while absorption in the 675-690 nm interval decreases markedly. These changes are analyzed in terms of a Gaussian decomposition description in which the eight subbands display a temperature-dependent broadening in agreement with the weak electron-phonon coupling demonstrated for other antenna chlorophyll spectral forms. In this way, we demonstrate that increased chlorophyll b binding leads to increased absorption intensity associated with the subbands at 640, 648, 655, and 660 nm and decreased intensity for the long wavelength subbands at 678 and 684 nm. The wavelength position of all subbands is unchanged. The above data are interpreted to indicate that CP29 has eight chlorophyll binding sites, many or all of which can be occupied by either chlorophyll a or chlorophyll b according to the conditions in which pigment binding occurs. Chlorophyll b absorption is primarily associated with four subbands located at 640, 648, 655, and 660 nm. The invariance of the wavelength position of the absorption bands in recombinant products with different chlorophyll a/b binding stoichiometries is discussed in terms of the mechanism involved in the formation of spectral bands. We conclude that pigment-protein interactions dominate in the determination of spectral heterogeneity with probably only minor effects on absorption associated with pigment-pigment interactions.

Apoproteins↗
PubMed1994

Chlorophyll regulates accumulation of the plastid-encoded chlorophyll proteins P700 and D1 by increasing apoprotein stability.

Chlorophyll protein accumulation in barley (Hordeum vulgare L.) chloroplasts is controlled posttranscriptionally by light-induced formation of chlorophyll a. The 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 presence of lincomycin, an inhibitor of translation initiation, to determine whether chlorophyll protein accumulation was regulated at the level of translation elongation. The 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 D1 translation intermediates to a small extent and greatly increased D1 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.

Apoproteins↗
PubMed1992

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

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 novo 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 microM aurintricarboxylic acid or 20 microM 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.

Aminoglycosides↗
PubMed1990

In vitro synthesis of chlorophyll a in the dark triggers accumulation of chlorophyll a apoproteins in barley etioplasts.

An in vitro translation system using lysed etioplasts was developed to test if the accumulation of plastid-encoded chlorophyll a apoproteins is dependent on the de novo synthesis of chlorophyll a. The P700 apoproteins, CP47 and CP43, were not radiolabeled in pulsechase translation assays employing lysed etioplasts in the absence of added chlorophyll precursors. When chlorophyllide a plus phytylpyrophosphate were added to lysed etioplast translation assays in the dark, chlorophyll a was synthesized and radiolabeled P700 apoproteins, CP47 and CP43, and a protein which comigrates with D1 accumulated. Chlorophyllide a or phytylpyrophosphate added separately to the translation assay in darkness did not induce chlorophyll a formation or chlorophyll a apoprotein accumulation. Chlorophyll a formation and chlorophyll a apoprotein accumulation were also induced in the lysed etioplast translation system by the photoreduction of protochlorophyllide to chlorophyllide a in the presence of exogenous phytylpyrophosphate. Accumulation of radiolabeled CP47 was detectable when very low levels of chlorophyll a were synthesized de novo (less than 0.01 nmol/10(7) plastids), and radiolabel increased linearly with increasing de novo chlorophyll a formation. Higher levels of de novo synthesized chlorophyll a were required prior to detection of radiolabel incorporation into the P700 apoproteins and CP43 (greater than 0.01 nmol/10(7) plastids). Radiolabel incorporation into the P700 apoproteins, CP47 and CP43, saturated at a chlorophyll a concentration which corresponds to 50% of the etioplast protochlorophyllide content (0.06 nmol of chlorophyll a/10(7) plastids).

Apoproteins↗
PubMed1983

[Chlorophyll-protein complexes from green algae and higher plants. Identification of chlorophyll-containing bands in gel, using Chlamydomonas reinhardii mutants].

Three types of mutants (pigment, non-photosynthesizing and pigment non-photosynthesizing ones) were used to identify the chlorophyll-containing bands in gel slices. The pigment mutants with an impaired light-harvesting chlorophyll a/b-protein complex possess photochemically active reaction centers of photosystems and are capable of phototrophic growth. Using these mutants, the heterogeneity of the chlorophyll-containing bands, LH2 and LH3, in gel slices and the dependence of LH2 on chlorophyll a-protein and that of LH3 on chlorophyll b-protein in the light-harvesting complex were established. The non-photosynthesizing mutants with an inactive photosystem I (or II) are devoid of antennae forms of chlorophyll a and are not capable of phototrophic growth. Using these mutants, it was demonstrated that in gel slices the chlorophyll-containing band, CPI, corresponds to the chlorophyll a-protein complex of photosystem I, while CPII to the chlorophyll a-protein complex of photosystem II. It was also found that the presence of the chlorophyll-containing band, LH0 (CPIa) in gel slices correlates with the preservation of the light-harvesting complex and is independent of photosystem I. The spectral properties of chlorophyll complexes in gel slices are not identical to those of native chlorophyll. It was assumed that chloroplasts contain at least 4 types of chlorophyll proteins that are controlled by independent genes.

Chlamydomonas↗
PubMed1994

Properties of synthesis of chlorophyll a from chlorophyll b in cucumber etioplasts.

Chlorophyll a accumulated when chlorophyllide b was incubated with isolated cucumber etioplasts in the dark. When [14C]chlorophyllide b was used as the substrate for chlorophyll synthesis, [14C]chlorophyll a was formed, showing that chlorophyll a was synthesized from the exogenously added chlorophyllide b, not by light-independent reduction of endogenous protochlorophyllide. The reaction studied showed an optimal pH of 7.5 and required both the soluble and membrane fractions of etioplasts together with ATP. Time course experiments showed that chlorophyll a began to accumulate later than chlorophyll b. Chlorophyllide b esterified with geranylgeraniol accumulated first, but there was little accumulation of chlorophyll a with an unhydrogenated prenyl side chain. No chlorophyllide a was detected during incubation. These observations indicate that esterified chlorophyll b was converted to chlorophyll a. This conversion would play an important role in the use of chlorophyll b for the synthesis of chlorophyll a in the reconstruction of photosystems.

Chlorophyll↗
PubMed1981

Light-harvesting systems of brown algae and diatoms. Isolation and characterization of chlorophyll a/c and chlorophyll a/fucoxanthin pigment-protein complexes.

The present study examined the protein associations and energy transfer characteristics of chlorophyll c and fucoxanthin which are the major light-harvesting pigments in the brown and diatomaceous algae. It was demonstrated that sodium dodecyl sulfate (SDS)-solubilized photosynthetic membranes of these species when subjected to SDS polyacrylamide gel electrophoresis yielded three spectrally distinct pigment-protein complexes. The slowest migrating zone was identical to complex I, the SDS-altered form of the P-700 chlorophyll a-protein. The zone of intermediate mobility contained chlorophyll c and chlorophyll a in a molar ratio of 2 : 1, possessed no fucoxanthin, and showed efficient energy transfer from chlorophyll c to chlorophyll a. The fastest migrating pigment-protein zone contained fucoxanthin and chlorophyll a, possessed no chlorophyll c, and showed efficient energy transfer from fucoxanthin to chlorophyll a. It is demonstrated that the chlorophyll a/c-protein and the chlorophyll a/fucoxanthin-protein complexes are common to the brown algae and diatoms examined, and likely share similar roles in the photosynthetic units of these species.

Carotenoids↗
PubMed1983

Chlorophyll a biosynthetic routes and chlorophyll a chemical heterogeneity in plants.

A six-branched chlorophyll a biosynthetic pathway instead of a four-branched pathway has been proposed as being responsible for the formation of chlorophyll a in green plants. The several biosynthetic routes that make up the pathway have been described as leading to the formation of ten chemically different groups of chlorophyll a species. The latter differ from one another by one or more of the following modifications: (a) by having a vinyl or ethyl group at position 4 of the macrocycle, (b) by the nature of the long-chain fatty alcohols at position 7 of the macrocycle, and (c) by having a 6-membered lactone ring instead of a 5-membered cyclopentanone ring. The chemical structure of several of the metabolic intermediates of that pathway and of some of the chlorophyll a species have now been determined by primary chemical derivatization methods coupled to spectrofluorometric, nuclear magnetic resonance and mass spectral analyses. The formation of highly organized photosynthetic membranes in which some of the chlorophyll alpha molecules are specifically oriented is ascribed to the multiplicity of chlorophyll biosynthetic routes which result in the formation of multiple chlorophyll alpha chemical species. Proper orientation of chlorophyll in the photosynthetic membranes is visualized as being controlled by peripheral group modifications that either modulate the polarity of the Chl chromophore or control the magnitude of the net positive charge on the central Mg atom. Finally it is proposed that in addition to the proper orientation of chlorophyll a, chemical heterogeneity of the chlorophyll chromophores in the photosynthetic reaction centers is mandatory for efficient charge separation, and proper vectorial electron transfer.

Chlorophyll↗
PubMed1990

Chlorophyll regulates accumulation of the plastid-encoded chlorophyll apoproteins CP43 and D1 by increasing apoprotein stability.

Chlorophyll apoprotein accumulation in higher plant chloroplasts is controlled by light-dependent chlorophyll formation. Dark-grown plants lack chlorophyll and chlorophyll apoproteins. However, the plastid genes encoding the chlorophyll apoproteins are transcribed; chlorophyll apoprotein mRNA accumulates and associates with polysomes in plastids of dark-grown plants. Pulse-labeling assays revealed a population of short-lived proteins in plastids of dark-grown plants. One of these transiently labeled proteins was CP43, a chlorophyll apoprotein associated with photosystem II. Pulse-chase assays showed that newly synthesized CP43 was rapidly degraded in plastids of dark-grown plants, which lack chlorophyll. In contrast, CP43 synthesized in plastids from illuminated plants was stable. The synthesis of D1, a chlorophyll apoprotein of the photosystem II reaction center, was also analyzed in plastids of dark-grown and illuminated plants. Radiolabel accumulation into full-length D1 was only detected in plastids of illuminated plants. However, D1 translation intermediates of 15-25 kDa were detected in both plastid populations. Pulse-chase assays showed that the 15- to 25-kDa D1 translation products were precursors of mature D1 in plastids of illuminated plants. In contrast, in plastids of dark-grown plants, the 15- to 25-kDa translation intermediates were converted into a 23-kDa polypeptide previously suggested to be a proteolytic product of D1. These results indicate that chlorophyll produced in illuminated plants stabilizes D1 nascent polypeptides, which allows accumulation of mature D1.

Apoproteins↗