Accumulation of plastid lipid‐associated proteins (fibrillin/CDSP34) upon oxidative stress, ageing and biotic stress in Solanaceae and in response to drought in other species

Langenkämper, Georg; Manac′h, Nathalie; Broin, Mélanie; Cuiné, Stéphan; Bécuwe, Noëlle; Kuntz, Marcel; Rey, Pascal

doi:10.1093/jexbot/52.360.1545

Cited by 95 publications

(63 citation statements)

References 32 publications

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“…Two different fibrillins were identified: Fibrillin-1 (At4g0420) was present in gel spot at pI 4.4; MW 28 kDa, whereas Fibrillin-6 (At3g23400) was identified in the gel spots at pI 4.6; MW 27 kDa and at pI 4.7; MW 27 kDa. Fibrillins are plastid-lipid associated proteins (PAPs) that belong to the plastoglobulin family and are induced by oxidative stress [42,43]. Fibrillins contain a conserved lipocalin signature involved in transport of small hydrophobic molecules (e.g., porphyrins) [24].…”

Section: Discussionmentioning

confidence: 99%

Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Galetskiy

Susnea

Reiser

et al. 2008

J. Am. Soc. Mass Spectrom.

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Structure and dynamics of membrane-bound light-harvesting pigment-protein complexes (LHCs), which collect and transmit light energy for photosynthesis and thereby play an essential role in the regulation of photosynthesis and photoprotection, were identified and characterized using high-resolution Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS). LHCs from photosystem n (LHCn) were isolated from the thylakoid membrane of Arabidopsis thaliana leaves after light stress treatment using sucrose density gradient centrifugation, and separated by gel-filtration into LHCn subcomplexes. Using reversed-phase high-performance liquid chromatography and two-dimensional (2D) gel electrophoresis, the LHCn proteins, Lhcbl-6 and fibrillins, were efficiently separated and identified by FIICR-MS. Some of the LHcn subcomplexes were shown to migrate from photosystem n to photosystem I as a result of short-term adaptation to changes in light intensity. In the mobile LHCn subcomplexes, decreased levels of fibrillins and a modified composition of LHCn protein isoforms were identified compared to the tightly bound LHcn subcomplexes. In addition, FTICR-MS analysis revealed several oxidative modifications of LHCn proteins. A number of protein spots in 2D gels were found to contain a mixture of proteins, illustrating the feasibility of high-resolution mass spectrometry to identify proteins that remain unseparated in 2D gels even upon extended pH gradients. (J

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Section: Discussionmentioning

confidence: 99%

Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Galetskiy

Susnea

Reiser

et al. 2008

J. Am. Soc. Mass Spectrom.

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“…In addition, the expression of PGL genes has been shown to be modulated by diverse stress stimuli such as exposure to reactive oxygen species [48,49] or ozone [50], ABA induction [51,52], wounding [3,48,50,53], bacterial infection [49] and a variety of other environmental stress conditions [3,48,50,51,[53][54][55]. Systematic and quantitative comparative proteomics have shown that the predominant change in the Arabidopsis peripheral thylakoid proteome upon light stress treatment is the several-fold up-regulation of plastoglobule associated proteins [56].…”

Section: Involvement Of Plastoglobules In Stress Responsementioning

confidence: 99%

Plastoglobules: versatile lipoprotein particles in plastids

Bréhélin

Kessler

Wijk

2007

Trends in Plant Science

243

157

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Plastoglobules are plastid-localized lipoprotein particles that contain tocopherols and other lipid isoprenoidderived metabolites, as well as structural proteins named plastoglobulins. Surprisingly, recent publications show that plastoglobules contain enzymes involved in the metabolism of these secondary metabolites, as well as enzymes of unknown function. The size and number of plastoglobules vary during plastid development and differentiation, and strongly increase during light stress, senescence and in mutants blocked in thylakoid formation. Given that plastoglobules are contiguous with the outer lipid leaflet of the thylakoid membrane, it is highly plausible that a function of plastoglobules is the active channeling of lipid molecules and lipid breakdown products. Understanding the function of plastoglobules should provide a foundation for improving the nutritional value and yield of plants.History of plastoglobule research and discovery Early electron microscopic studies revealed the presence of 'osmiophilic globuli' inside chloroplasts ( Figure 1) and chromoplasts, as well as other plastid types [1]. The diameter of these bodies, later termed plastoglobules, ranges from 30 nm to 5 mm. These plastoglobules could be conveniently isolated by flotation density centrifugation because of their relatively high lipid content [1,2]. The lipid composition of plastoglobules has been determined in several plant species -it consists mainly of prenyl-quinones and neutral lipids. Plastoglobules qualify as lipoprotein particles because they have been reported to associate with proteins. Members of the plastoglobulin family (also called fibrillin or PAP for plastid lipid-associated protein) [3], were the first known genuine plastoglobule protein components. In addition to vascular plants, plastoglobules are found in non-vascular species such as moss [4] and algae [5,6]. Interestingly, carotenoid-rich plastoglobule-like structures constitute the eyespot structure of Chlamydomonas reinhardtii, the proteome of which has been shown to contain members of the plastoglobulin family [6]. In cyanobacteria, the presence of 'lipid droplets' among the thylakoids has been reported [7]. The exact identity of these lipid droplets has not been defined; however, the presence of at least two plastoglobulin homologs in the genome of Synechocystis PCC6803 suggests that they could be plastoglobules.Although plastoglobules were largely viewed as passive lipid and carotenoid storage particles, their varying size in different species, plastid types and developmental stages suggested a more dynamic role. Moreover, correlative evidence suggested that plastoglobules are involved in thylakoid development as well as disassembly: (i) etioplasts with poorly developed thylakoids have more plastoglobules than are found in chloroplasts, but the plastoglobule abundance decreased during thylakoid biogenesis [8-10]; (ii) in senescent chloroplasts, during thylakoid disassembly, plastoglobules enlarge and accumulate [9,11,12]; (iii) several thylakoid biogenesis...

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“…Taken together, the results strongly argue for a specific binding of ABI2 to the fibrillin preprotein in vitro and in vivo. Fibrillins are inducible proteins, and their expression is upregulated by drought, cold, and oxidative and salt stress (3)(4)(5)(6). These stress conditions involve ABA as a signal, and, hence, we examined whether ABA is able to regulate fibrillin gene expression.…”

Section: Identification Of Prefibrillin As An Interacting Partner Of mentioning

confidence: 99%

“…They have been primarily characterized from chromoplasts of tomato and pepper fruits and are known to accumulate during abiotic stress in plastids e.g., inflicted by high light, cold, and drought (3)(4)(5), and also during pathogen infection (6). The family of fibrillin-like proteins is unique to plants, and the members contain a hydrophobic domain that associates with or anchors within lipids (7).…”

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confidence: 99%

Fibrillin expression is regulated by abscisic acid response regulators and is involved in abscisic acid-mediated photoprotection

Yang

Sulpice

Himmelbach

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

113

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Fibrillins are lipid-binding proteins of plastids that are induced under abiotic stress conditions. In response to environmental stress, plants generate abscisic acid (ABA) as an endogenous signal. We show that ABA treatment and fibrillin accumulation enhance the tolerance of photosystem II toward light stress-triggered photoinhibition in Arabidopsis. ABA induces fibrillin accumulation, and the ABA response regulators ABI1 and ABI2 regulate fibrillin expression. The abundance of fibrillin transcripts was specifically reduced in the ABA-insensitive abi1 mutant but not in the abi2 mutant. However, leaves of abi2 revealed in comparison to WT and abi1 enhanced fibrillin levels, pointing to a posttranscriptional control mechanism. Protein interaction analysis identified the protein phosphatase ABI2 to target the preprotein of fibrillin. Interaction was abrogated either by deleting the signal peptide of prefibrillin or by the single amino acid exchange present in the phosphatase-deficient abi2 protein. Thus, ABI1 and ABI2 seem to control fibrillin expression that is involved in mediating ABAinduced photoprotection.ABI1 ͉ ABI2 ͉ abiotic stress ͉ photoinhibition ͉ light stress F ibrillins are plastid-associated lipid-binding proteins that are ubiquitous in plants (1, 2). They have been primarily characterized from chromoplasts of tomato and pepper fruits and are known to accumulate during abiotic stress in plastids e.g., inflicted by high light, cold, and drought (3-5), and also during pathogen infection (6). The family of fibrillin-like proteins is unique to plants, and the members contain a hydrophobic domain that associates with or anchors within lipids (7). Fibrillins associate with stromal lamellae of thylakoids and fibrillic carotenoid-containing structures of chromoplasts (3,8). A model for the fibrillic structures predicts a layer of fibrillin shielding polar lipids and carotenoids (1). In potato, the fibrillin C40.4 protein is specifically associated with the photosystem II (PSII) light-harvesting complex with a presumptive role in the modulation of photosynthetic efficiency (9). A posttranslational control of fibrillin accumulation by abscisic acid (ABA) was indicated by studies on ABA-deficient tomato that failed to accumulate fibrillin despite normal transcript levels (5). Although fibrillin is induced in response to abiotic stress, its role in stress responses and the molecular mechanism regulating its accumulation are still elusive.ABA plays a major role in regulating plant growth and development and mediating adaptations to environmental stress such as cold, drought, and salinity (10). ABA regulates ion channel activities involved in osmoregulation and stomatal closure and influences gene expression at the transcriptional and posttranscriptional levels (11,12). Key regulators of diverse ABA-mediated responses are ABI1 and ABI2. Both proteins are members of a larger family of plant protein phosphatases 2C (PP2Cs), several of which act negatively in a partially redundant manner on ABA responses (13-15). The...

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Accumulation of plastid lipid‐associated proteins (fibrillin/CDSP34) upon oxidative stress, ageing and biotic stress in Solanaceae and in response to drought in other species

Cited by 95 publications

References 32 publications

Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Structure and dynamics of photosystem II light-harvesting complex revealed by high-resolution FTICR mass spectrometric proteome analysis

Plastoglobules: versatile lipoprotein particles in plastids

Fibrillin expression is regulated by abscisic acid response regulators and is involved in abscisic acid-mediated photoprotection

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