The plant nuclear envelope

Rose, Annkatrin; Patel, Shalaka; Meier, Iris

doi:10.1007/s00425-003-1132-2

Cited by 41 publications

(28 citation statements)

References 113 publications

(104 reference statements)

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“…In yeast, animals, and plants, a close relationship between the 26S proteasome and the nuclear envelope has been found and is thought to play a role in monitoring the protein traffic between the cytosol and the nucleus (reviewed in ref. 48). The regulation of the 26S proteasome might thus be linked to the regulation of Ran.…”

Section: Figmentioning

confidence: 99%

New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii

Lemaire

Guillon

Maréchal

et al. 2004

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

235

189

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Proteomics were used to identify the proteins from the eukaryotic unicellular green alga Chlamydomonas reinhardtii that can be reduced by thioredoxin. These proteins were retained specifically on a thioredoxin affinity column made of a monocysteinic thioredoxin mutant able to form mixed disulfides with its targets. Of a total of 55 identified targets, 29 had been found previously in higher plants or Synechocystis, but 26 were new targets. Biochemical tests were performed on three of them, showing a thioredoxindependent activation of isocitrate lyase and isopropylmalate dehydrogenase and a thioredoxin-dependent deactivation of catalase that is redox insensitive in Arabidopsis. In addition, we identified a Ran protein, a previously uncharacterized nuclear target in a photosynthetic organism. The metabolic and evolutionary implications of these findings are discussed.O ur knowledge on redox regulation of various physiological processes through thiol-disulfide interchange with proteins of the thioredoxin (TRX) superfamily is rapidly progressing as genome-wide approaches and functional genomics studies are expanding. In the plant biology domain, thioredoxin-dependent regulation has been first discovered for chloroplastic enzymes involved in carbon assimilation (1). The completion of the sequencing of the Arabidopsis genome revealed that TRXs constituted a multigene family and led to the assumption that numerous TRX targets were still to be discovered (2-4). Thus, proteomic approaches aimed at identifying the largest possible number of TRX targets have been developed. The first attempts took advantage of the reaction mechanism of TRXs with their targets, in which a transient heterodisulfide forms between the reduced TRX and the oxidized protein, followed by the release of the reduced target due to the attack of the mixed disulfide by the second cysteine of TRX. Model studies showed that when this second cysteine was mutated, the heterodisulfide was stabilized (5, 6). This property was applied in vivo by transforming a TRX-null mutant yeast with a monocysteinic TRX and allowed isolating a peroxiredoxin (PRX) (7). Subsequently, monocysteinic TRX mutants were used in affinity chromatography to trap interacting proteins (8-11). Native TRX affinity columns also allowed retaining some targets by electrostatic interaction (12). Another technique was also developed that consists of a reduction of a crude soluble protein extract with reduced TRX followed by a separation of the proteins on a 2D gel after derivatization of the newly appeared thiols either with a fluorescent (13) or with a radioactive (14) reagent. In one case, both techniques have been applied in parallel (15), yielding similar results.Most of the disulfide proteomics have been led with higher plants: spinach (8, 10, 12), Arabidopsis (11, 14), or cereal grains (12). A single study was led with cyanobacteria and revealed targets mostly different from those of higher plants (16). The unicellular eukaryotic green alga Chlamydomonas reinhardtii possesses a TRX syste...

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Section: Figmentioning

confidence: 99%

New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii

Lemaire

Guillon

Maréchal

et al. 2004

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

235

189

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“…Nuclear degradation processes encompass chromatin events (i.e., chromatin condensation and DNA fragmentation) and nuclear envelope events (i.e., lobing of the nuclear surface and disassembly of nuclear pore complex) that occur simultaneously in the same cell (2,5). The structural organization of plant and animal nuclei is conserved (6), explaining why the morphological pattern of nuclear degradation is also conserved (2). However, the molecular composition of plant and animal nuclear envelopes is not conserved (6), implying that different molecular mechanisms are responsible for nuclear envelope events during PCD in plants.…”

mentioning

confidence: 99%

“…The structural organization of plant and animal nuclei is conserved (6), explaining why the morphological pattern of nuclear degradation is also conserved (2). However, the molecular composition of plant and animal nuclear envelopes is not conserved (6), implying that different molecular mechanisms are responsible for nuclear envelope events during PCD in plants.…”

mentioning

confidence: 99%

Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis

Bozhkov

Suárez

Filonova

et al. 2005

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

226

235

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Programmed cell death (PCD) is indispensable for eukaryotic development. In animals, PCD is executed by the caspase family of cysteine proteases. Plants do not have close homologues of caspases but possess a phylogenetically distant family of cysteine proteases named metacaspases. The cellular function of metacaspases in PCD is unknown. Here we show that during plant embryogenesis, metacaspase mcII-Pa translocates from the cytoplasm to nuclei in terminally differentiated cells that are destined for elimination, where it colocalizes with the nuclear pore complex and chromatin, causing nuclear envelope disassembly and DNA fragmentation. The cell-death function of mcII-Pa relies on its cysteine-dependent arginine-specific proteolytic activity. Accordingly, mutation of catalytic cysteine abrogates the proteolytic activity of mcII-Pa and blocks nuclear degradation. These results establish metacaspase as an executioner of PCD during embryo patterning and provide a functional link between PCD and embryogenesis in plants. Although mcII-Pa and metazoan caspases have different substrate specificity, they serve a common function during development, demonstrating the evolutionary parallelism of PCD pathways in plants and animals.embryo suspensor ͉ metacaspase ͉ nuclear degradation P rogrammed cell death (PCD) is indispensable for normal embryo development both in animals and in plants, where temporary, surplus, or aberrantly formed tissues and organs are removed for correct pattern formation (1, 2). The key morphogenetic event in plant embryogenesis is formation of the apicalbasal pattern via establishment of the proliferating embryo proper (apical) and the terminally differentiated suspensor (basal). Developmental programs of the embryo proper and the suspensor are closely coordinated, and imbalance causes embryonic defects or lethality (2-4). While the embryo proper gives rise to the plant, the suspensor functions during a brief period as a conduit of growth factors to the developing embryo and is subsequently eliminated by PCD (2). The terminal differentiation of the embryo suspensor is the earliest manifestation of cellular suicide in plant ontogenesis. However, the molecular mechanisms that regulate PCD in plant embryos are unknown.The nucleus is the major target of cell degradation machinery during PCD. Nuclear degradation processes encompass chromatin events (i.e., chromatin condensation and DNA fragmentation) and nuclear envelope events (i.e., lobing of the nuclear surface and disassembly of nuclear pore complex) that occur simultaneously in the same cell (2, 5). The structural organization of plant and animal nuclei is conserved (6), explaining why the morphological pattern of nuclear degradation is also conserved (2). However, the molecular composition of plant and animal nuclear envelopes is not conserved (6), implying that different molecular mechanisms are responsible for nuclear envelope events during PCD in plants.In animals, nuclear degradation during PCD is executed by a caspase family of cysteine proteases...

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“…Тем не менее, теломеры выполняют ряд важных функций, среди которых: сохранение целостности генома эукариотической клетки путем защиты от слияния концов хромосом [5], обеспече-ние фиксации хромосом к ядерной оболочке [9], обеспечение стабилизации поврежденных и разор-ванных концов хромосом [10], влияние на экспрес-сию генов [11], определение репликационного потен-циала клетки [12] и многие другие.…”

Section: Telomere Length and Atherosclerosisunclassified

Telomere Length and Atherosclerosis

Драпкина¹,

Shepel²

2016

Russ J Cardiol

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The plant nuclear envelope

Cited by 41 publications

References 113 publications

New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii

New thioredoxin targets in the unicellular photosynthetic eukaryote Chlamydomonas reinhardtii

Cysteine protease mcII-Pa executes programmed cell death during plant embryogenesis

Telomere Length and Atherosclerosis

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