Peroxisome division and proliferation in plants

2010 ◽  
Vol 38 (3) ◽  
pp. 817-822 ◽  
Author(s):  
Kyaw Aung ◽  
Xinchun Zhang ◽  
Jianping Hu
Keyword(s):  
Red Light ◽  
Specific Protein ◽  
Development Research ◽  
Phytochrome A ◽  
Division 1 ◽  
Evolutionarily Conserved ◽  
Organelle Division ◽  
Specific Factors ◽  
Related Proteins ◽  
Peroxisome Division

Peroxisomes are eukaryotic organelles with crucial functions in development. Plant peroxisomes participate in various metabolic processes, some of which are co-operated by peroxisomes and other organelles, such as mitochondria and chloroplasts. Defining the complete picture of how these essential organelles divide and proliferate will be instrumental in understanding how the dynamics of peroxisome abundance contribute to changes in plant physiology and development. Research in Arabidopsis thaliana has identified several evolutionarily conserved major components of the peroxisome division machinery, including five isoforms of PEROXIN11 proteins (PEX11), two dynamin-related proteins (DRP3A and DRP3B) and two FISSION1 proteins (FIS1A/BIGYIN and FIS1B). Recent studies in our laboratory have also begun to uncover plant-specific factors. DRP5B is a dual-localized protein that is involved in the division of both chloroplasts and peroxisomes, representing an invention of the plant/algal lineage in organelle division. In addition, PMD1 (peroxisomal and mitochondrial division 1) is a plant-specific protein tail anchored to the outer surface of peroxisomes and mitochondria, mediating the division and/or positioning of these organelles. Lastly, light induces peroxisome proliferation in dark-grown Arabidopsis seedlings, at least in part, through activating the PEX11b gene. The far-red light receptor phyA (phytochrome A) and the transcription factor HYH (HY5 homologue) are key components in this signalling pathway. In summary, pathways for the division and proliferation of plant peroxisomes are composed of conserved and plant-specific factors. The sharing of division proteins by peroxisomes, mitochondria and chloroplasts is also suggesting possible co-ordination in the division of these metabolically associated plant organelles.

Far-Red Light Blocks Greening of Arabidopsis Seedlings via a Phytochrome A: Mediated Change in Plastid Development

1996 ◽  
Vol 8 (4) ◽  
pp. 601 ◽  
Author(s):  
Simon A. Barnes ◽  
Naoko K. Nishizawa ◽  
Ronaldo B. Quaggio ◽  
Garry C. Whitelam ◽  
Nam-Hai Chua
Keyword(s):  
Red Light ◽  
Phytochrome A ◽  
Plastid Development

scholarly journals An evolutionarily conserved U5 snRNP-specific protein is a GTP-binding factor closely related to the ribosomal translocase EF-2

1997 ◽  
Vol 16 (13) ◽  
pp. 4092-4106 ◽  
Author(s):  
Patrizia Fabrizio ◽  
Bernhard Laggerbauer ◽  
Jürgen Lauber ◽  
William S. Lane ◽  
Reinhard Lührmann
Keyword(s):  
Specific Protein ◽  
Gtp Binding ◽  
Binding Factor ◽  
Evolutionarily Conserved

A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene

1988 ◽  
Vol 8 (1) ◽  
pp. 371-380
Author(s):  
T W McMullin ◽  
R L Hallberg
Keyword(s):  
Escherichia Coli ◽  
Tetrahymena Thermophila ◽  
Mitochondrial Protein ◽  
Cross Reactivity ◽  
Macromolecular Complexes ◽  
E Coli ◽  
Groel Gene ◽  
Evolutionarily Conserved ◽  
Associated Proteins ◽  
Related Proteins

We recently reported that a Tetrahymena thermophila 58-kilodalton (kDa) mitochondrial protein (hsp58) was selectively synthesized during heat shock. In this study, we show that hsp58 displayed antigenic similarity with mitochondrially associated proteins from Saccharomyces cerevisiae (64 kDa), Xenopus laevis (60 kDa), Zea mays (62 kDa), and human cells (59 kDa). Furthermore, a 58-kDa protein from Escherichia coli also exhibited antigenic cross-reactivity to an antiserum directed against the T. thermophila mitochondrial protein. The proteins from S. cerevisiae and E. coli antigenically related to hsp58 were studied in detail and found to share several other characteristics with hsp58, including heat inducibility and the property of associating into distinct oligomeric complexes. The T. thermophila, S. cerevisiae, and E. coli macromolecular complexes containing these related proteins had similar sedimentation characteristics and virtually identical morphologies as seen with the electron microscope. The distinctive properties of the E. coli homolog to T. thermophila hsp58 indicate that it is most likely the product of the groEL gene.

Dynamics of the processes leading to the acquisition of sensitivity to very low fluence of photons inDatura feroxseeds

2013 ◽  
Vol 23 (4) ◽  
pp. 233-239
Author(s):  
Gabriela Alejandra Auge ◽  
Lucila de Miguel
Keyword(s):  
Physiological State ◽  
Red Light ◽  
Light Sensitivity ◽  
Growth Potential ◽  
Soil Tillage ◽  
Phytochrome A ◽  
Light Stimulation ◽  
Endosperm Weakening ◽  
Signalling Network ◽  
Stimulation Of

AbstractSoil tillage operations stimulate germination of buried seeds in cultivated lands, allowing them to perceive light as a germination-promoting factor. The time of burial and the effect of changing environmental factors affect the physiological state of the seeds, which may lead to an extreme light-sensitivity and very low fluence response (VLFR) through phytochrome A. This paper describes the influence of the progressive process of dormancy breakage, which is accompanied by the acquisition of extreme light-sensitivity, on processes associated with endosperm weakening and embryo growth potential in the VLFR-mediated promotion ofDatura feroxseed germination. Our results show that endosperm weakening is mainly limited by β-mannosidase enzyme activity after far-red light stimulation, which is highly dependent on the dormancy level of the seeds. In addition, stimulation of the embryo growth potential by far-red irradiation did not require an extreme light-sensitivity to very low fluence of photons to reach its maximum response, and it was not completely correlated with expansin gene expression in the embryo. Our work indicates that responses of endosperm weakening and embryo growth potential to far-red irradiation, dependent on dormancy level, have different requirements for stimulation by the signalling network initiated by phytochrome A during the course of the very low fluence response inDatura feroxseeds.

scholarly journals Multidimensional Proteomics Identifies Declines in Protein Homeostasis and Mitochondria as Early Signals for Normal Aging and Age-associated Disease in Drosophila

2019 ◽  
Vol 18 (10) ◽  
pp. 2078-2088 ◽  
Author(s):  
Lu Yang ◽  
Ye Cao ◽  
Jing Zhao ◽  
Yanshan Fang ◽  
Nan Liu ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Dynamics ◽  
Isotope Labeling ◽  
Specific Protein ◽  
Normal Aging ◽  
Protein Homeostasis ◽  
Age Related ◽  
Muscle Tissues ◽  
Proteomic Study ◽  
Related Proteins

Aging is characterized by a gradual deterioration in proteome. However, how protein dynamics that changes with normal aging and in disease is less well understood. Here, we profiled the snapshots of aging proteome in Drosophila, from head and muscle tissues of post-mitotic somatic cells, and the testis of mitotically-active cells. Our data demonstrated that dysregulation of proteome homeostasis, or proteostasis, might be a common feature associated with age. We further used pulsed metabolic stable isotope labeling analysis to characterize protein synthesis. Interestingly, this study determined an age-modulated decline in protein synthesis with age, particularly in the pathways related to mitochondria, neurotransmission, and proteostasis. Importantly, this decline became dramatically accelerated in Pink1 mutants, a Drosophila model of human age-related Parkinson's disease. Taken together, our multidimensional proteomic study revealed tissue-specific protein dynamics with age, highlighting mitochondrial and proteostasis-related proteins. We suggest that declines in proteostasis and mitochondria early in life are critical signals prior to the onset of aging and aging-associated diseases.

scholarly journals Regulated protein stabilization underpins the functional interplay among basal body components in Trypanosoma brucei

2019 ◽  
Vol 295 (3) ◽  
pp. 729-742
Author(s):  
Kieu T. M. Pham ◽  
Ziyin Li
Keyword(s):  
Trypanosoma Brucei ◽  
Basal Body ◽  
Super Resolution ◽  
Specific Protein ◽  
Protein Stabilization ◽  
Structured Illumination ◽  
Human Parasite ◽  
Evolutionarily Conserved ◽  
Body Components ◽  
Super Resolution Microscopy

The basal body in the human parasite Trypanosoma brucei is structurally equivalent to the centriole in animals and functions in the nucleation of axonemal microtubules in the flagellum. T. brucei lacks many evolutionarily conserved centriolar protein homologs and constructs the basal body through unknown mechanisms. Two evolutionarily conserved centriole/basal body cartwheel proteins, TbSAS-6 and TbBLD10, and a trypanosome-specific protein, BBP65, play essential roles in basal body biogenesis in T. brucei, but how they cooperate in the regulation of basal body assembly remains elusive. Here using RNAi, endogenous epitope tagging, immunofluorescence microscopy, and 3D-structured illumination super-resolution microscopy, we identified a new trypanosome-specific protein named BBP164 and found that it has an essential role in basal body biogenesis in T. brucei. Further investigation of the functional interplay among BBP164 and the other three regulators of basal body assembly revealed that BBP164 and BBP65 are interdependent for maintaining their stability and depend on TbSAS-6 and TbBLD10 for their stabilization in the basal body. Additionally, TbSAS-6 and TbBLD10 are independent from each other and from BBP164 and BBP65 for maintaining their stability in the basal body. These findings demonstrate that basal body cartwheel proteins are required for stabilizing other basal body components and uncover that regulation of protein stability is an unusual control mechanism for assembly of the basal body in T. brucei.

scholarly journals Peroxisome division in the yeast Yarrowia lipolytica is regulated by a signal from inside the peroxisome

2003 ◽  
Vol 162 (7) ◽  
pp. 1255-1266 ◽  
Author(s):  
Tong Guo ◽  
Yuriy Y. Kit ◽  
Jean-Marc Nicaud ◽  
Marie-Therese Le Dall ◽  
S. Kelly Sears ◽  
...  
Keyword(s):  
Yarrowia Lipolytica ◽  
Matrix Proteins ◽  
Peroxisomal Protein ◽  
Organelle Division ◽  
The Matrix ◽  
Membrane Bound ◽  
Complete Set ◽  
Acyl Coa Oxidase ◽  
Peroxisome Division ◽  
Yeast Yarrowia Lipolytica

We describe an unusual mechanism for organelle division. In the yeast Yarrowia lipolytica, only mature peroxisomes contain the complete set of matrix proteins. These mature peroxisomes assemble from several immature peroxisomal vesicles in a multistep pathway. The stepwise import of distinct subsets of matrix proteins into different immature intermediates along the pathway causes the redistribution of a peroxisomal protein, acyl-CoA oxidase (Aox), from the matrix to the membrane. A significant redistribution of Aox occurs only in mature peroxisomes. Inside mature peroxisomes, the membrane-bound pool of Aox interacts with Pex16p, a membrane-associated protein that negatively regulates the division of early intermediates in the pathway. This interaction inhibits the negative action of Pex16p, thereby allowing mature peroxisomes to divide.

Spatio-temporal expression analysis of two kinds of chemical communication-related proteins in the worker bee Apis cerana cerana Fabricius (Hymenoptera: Apidae)

2009 ◽  
Vol 6 (2) ◽  
pp. 147-152
Author(s):  
Li Hong-Liang ◽  
Zhang Ya-Li ◽  
Wang Hai-Yan ◽  
Gao Qi-Kang ◽  
Cheng Jia-An
Keyword(s):  
Chemical Communication ◽  
Apis Cerana ◽  
Specific Protein ◽  
Apis Cerana Cerana ◽  
Body Parts ◽  
Chemosensory Protein ◽  
Gene Coding ◽  
Intimate Relation ◽  
Spatio Temporal ◽  
Related Proteins

AbstractThe spatio-temporal expressed profiles of two kinds of chemical communication-related protein genes, the odorant-binding protein of Ac-ASP2 and chemosensory protein of Ac-ASP3, were identified by real-time polymerase chain reaction (PCR). Results obtained using the 2−ΔΔCt method showed that Ac-ASP2 was a gene coding antenna-specific protein that did not express in larvae and pupae, but had discontinuous high abundance periods at 1, 9, 15, 27 and 30 days. The expressing abundance at such periods was at least ten times higher than that at other periods. From the distribution of Ac-ASP3 mRNA observed in different tissues, the transcript levels seemed to be higher in the wings, abdomen and thorax (of order ~106), and lower in the legs, antennae and head (of order ~105). From highest to lowest, the original copy number was found in the various body parts in the following order: wings, abdomen, thorax, legs, antenna, and head. The results suggest that Ac-ASP3 has an intimate relation with the chemosensory behaviour of wings and abdomen in Apis cerana cerana.

scholarly journals Phosphorylation of FAR-RED ELONGATED HYPOCOTYL1 Is a Key Mechanism Defining Signaling Dynamics of Phytochrome A under Red and Far-Red Light in Arabidopsis

2012 ◽  
Vol 24 (5) ◽  
pp. 1907-1920 ◽  
Author(s):  
Fang Chen ◽  
Xiarong Shi ◽  
Liang Chen ◽  
Mingqiu Dai ◽  
Zhenzhen Zhou ◽  
...  
Keyword(s):  
Red Light ◽  
Phytochrome A ◽  
Signaling Dynamics
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