Synthesis of Two Chromoplast-Specific Proteins During Fruit Development in <i>Capsicum annuum</i>

Newman, L.; Hadjeb, Noureddine; Price, Colin

doi:10.1104/pp.91.2.455

Cited by 38 publications

(30 citation statements)

References 8 publications

(16 reference statements)

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“…Total chromoplasts (Fig. 3, lane 1) contained the two major chromoplast proteins, ChrA (53 kD) and ChrB (35 kD), which comprise 30% and 10% of red pepper chromoplast protein, respectively (Hadjeb et al, 1988;Newman et al, 1989). In agreement with the model that ChrB is peripherally associated with the lipid monolayer of fibrils, ChrB cofractionated with stroma and membranes, with the majority in the stroma (Fig.…”

Section: Isolation Of Intact Mature Red Bell Pepper Chromoplastssupporting

confidence: 67%

Red Bell Pepper Chromoplasts Exhibit in Vitro Import Competency and Membrane Targeting of Passenger Proteins from the Thylakoidal Sec and ΔpH Pathways but Not the Chloroplast Signal Recognition Particle Pathway1

Summer

Cline

1999

Plant Physiology

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Chloroplast to chromoplast development involves new synthesis and plastid localization of nuclear-encoded proteins, as well as changes in the organization of internal plastid membrane compartments. We have demonstrated that isolated red bell pepper (Capsicum annuum) chromoplasts contain the 75-kD component of the chloroplast outer envelope translocon (Toc75) and are capable of importing chloroplast precursors in an ATP-dependent fashion, indicating a functional general import apparatus. The isolated chromoplasts were able to further localize the 33-and 17-kD subunits of the photosystem II O 2 -evolution complex (OE33 and OE17, respectively), lumen-targeted precursors that utilize the thylakoidal Sec and ⌬pH pathways, respectively, to the lumen of an internal membrane compartment. Chromoplasts contained the thylakoid Sec component protein, cpSecA, at levels comparable to chloroplasts. Routing of OE17 to the lumen was abolished by ionophores, suggesting that routing is dependent on a transmembrane ⌬pH. The chloroplast signal recognition particle pathway precursor major photosystem II light-harvesting chlorophyll a/b protein failed to associate with chromoplast membranes and instead accumulated in the stroma following import. The Pftf (plastid fusion/translocation factor), a chromoplast protein, integrated into the internal membranes of chromoplasts during in vitro assays, and immunoblot analysis indicated that endogenous plastid fusion/translocation factor was also an integral membrane protein of chromoplasts. These data demonstrate that the internal membranes of chromoplasts are functional with respect to protein translocation on the thylakoid Sec and ⌬pH pathways.Plastids are developmentally related organelles capable of interconversion among a variety of structurally and biochemically distinct forms in response to both environmental and tissue-specific cues (Whatley, 1978;Thomson and Whatley, 1980). Formation of chromoplasts in many fruits is one striking example of this plasticity. Heavily pigmented, photosynthetically inactive chromoplasts frequently develop from chloroplasts during ripening. This conversion involves dramatic changes in the organization and composition of the internal plastid compartment, which include the loss of proteins involved in carbon fixation in the stroma and replacement with chromoplastspecific proteins, the breakdown of the photosynthetic thylakoid membranes and loss of proteins involved in light capture and electron transfer, and, in some cases, the formation of new membranes (Spurr and Harris, 1968; Camara and Brangeon, 1981;Piechulla et al., 1987;Kuntz et al., 1989).Chromoplast formation is an active rather than simply a degradative process. New proteins, specific to or enhanced in chromoplasts, are synthesized and compartmentalized in the plastid (Camara et al., 1995;Price et al., 1995). Most chromoplast proteins are predicted to be nuclear encoded, translated on cytoplasmic ribosomes, and posttranslationally imported into the plastid, as are nuclear-encoded chloroplast protein...

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Section: Isolation Of Intact Mature Red Bell Pepper Chromoplastssupporting

confidence: 67%

Red Bell Pepper Chromoplasts Exhibit in Vitro Import Competency and Membrane Targeting of Passenger Proteins from the Thylakoidal Sec and ΔpH Pathways but Not the Chloroplast Signal Recognition Particle Pathway1

Summer

Cline

1999

Plant Physiology

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“…The appearance of two chromoplast-specific proteins, designated ChrA and ChrB, has been documented previously (Hadjeb et al, 1988;Newman et al, 1989). Similarity in size between fibrillin and the 35-kD membrane protein ChrB, as well as in their time course of appearance, raises the possibility that these two proteins are related or identical.…”

Section: Discussionmentioning

confidence: 79%

Fibril assembly and carotenoid overaccumulation in chromoplasts: a model for supramolecular lipoprotein structures.

et al. 1994

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Chromoplast development in ripening bell pepper fruits is characterized by a massive synthesis of carotenoid pigments, resulting in their distinctlve red color. We have shown that 95% of these pigments accumulate in chromoplasts in speclfic lipoprotein fibrils. In addltion to carotenoids, purified fibrils contain galactolipids, phospholipids, and a single, 32-kD protein, designated fibrillin, which has antigenically related counterparts in other species. Fibrlls were reconstltuted in vitro when purified fibrillin was combined with carotenoids and polar llpids in the same stoichlometrlc ratlo found in fibrils in vivo. Antibodies dlrected against fibrillin were used to isolate a fibrillin cDNA clone and, in immunological studies, to follow its accumulation during the chloroplast-tothromoplast transltlon under different condltions. A model for fibril amhitecture is proposed wherein carotenoids accumulate in the center of the fibrils and are surrounded by a layer of polar lipids, which in turn are surrounded by an outer layer of fibrillin. Topological analysis of purlfied fibrils verified this structure. Collectively, these results suggest that the process of fibrll self-assembly in chromoplasts 1s an example of a general phenomenon shared among cells that target excess membrane llpids into deposit structures to avoid their destabilizing or toxic effects. In addition, we have shown that abscisic acid stimulates this phenomenon in chromoplasts, whereas gibberellic acid and auxin delay it.

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“…They were first identified in fibrils, the thread-like structures involved in carotenoid storage in the chromoplasts of bell pepper (Capsicum annuum) fruit (Newman et al, 1989;Deruère et al, 1994), and were called fibrillins because of their high abundance in fibrils. Members of the fibrillin protein family have been given many different names over the years, including plastid-lipid-associated protein (Pozueta-Romero et al, 1997;Ting et al, 1998), chromoplast-specific carotenoidassociated protein (Vishnevetsky et al, 1996), and plastoglobulins (Kessler et al, 1999).…”

Section: Introductionmentioning

confidence: 99%

Fibrillin 5 Is Essential for Plastoquinone-9 Biosynthesis by Binding to Solanesyl Diphosphate Synthases in Arabidopsis

2015

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Fibrillins are lipid-associated proteins in plastids and are ubiquitous in plants. They accumulate in chromoplasts and sequester carotenoids during the development of flowers and fruits. However, little is known about the functions of fibrillins in leaf tissues. Here, we identified fibrillin 5 (FBN5), which is essential for plastoquinone-9 (PQ-9) biosynthesis in Arabidopsis thaliana. Homozygous fbn5-1 mutations were seedling-lethal, and XVE:FBN5-B transgenic plants expressing low levels of FBN5-B had a slower growth rate and were smaller than wild-type plants. In chloroplasts, FBN5-B specifically interacted with solanesyl diphosphate synthases (SPSs) 1 and 2, which biosynthesize the solanesyl moiety of PQ-9. Plants containing defective FBN5-B accumulated less PQ-9 and its cyclized product, plastochromanol-8, but the levels of tocopherols were not affected. The reduced PQ-9 content of XVE:FBN5-B transgenic plants was consistent with their lower photosynthetic performance and higher levels of hydrogen peroxide under cold stress. These results indicate that FBN5-B is required for PQ-9 biosynthesis through its interaction with SPS. Our study adds FBN5 as a structural component involved in the biosynthesis of PQ-9. FBN5 binding to the hydrophobic solanesyl moiety, which is generated by SPS1 and SPS2, in FBN5-B/SPS homodimeric complexes stimulates the enzyme activity of SPS1 and SPS2.

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Synthesis of Two Chromoplast-Specific Proteins During Fruit Development in Capsicum annuum

Cited by 38 publications

References 8 publications

Red Bell Pepper Chromoplasts Exhibit in Vitro Import Competency and Membrane Targeting of Passenger Proteins from the Thylakoidal Sec and ΔpH Pathways but Not the Chloroplast Signal Recognition Particle Pathway1

Red Bell Pepper Chromoplasts Exhibit in Vitro Import Competency and Membrane Targeting of Passenger Proteins from the Thylakoidal Sec and ΔpH Pathways but Not the Chloroplast Signal Recognition Particle Pathway1

Fibril assembly and carotenoid overaccumulation in chromoplasts: a model for supramolecular lipoprotein structures.

Fibrillin 5 Is Essential for Plastoquinone-9 Biosynthesis by Binding to Solanesyl Diphosphate Synthases in Arabidopsis

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