Identification And Characterization Of A Novel Cap Binding Protein From Arabidopsis Thaliana And Of The Wheat Eukaryotic Initiation Factor Eif4g
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Identification And Characterization Of A Novel Cap Binding Protein From Arabidopsis Thaliana And Of The Wheat Eukaryotic Initiation Factor Eif4g
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Author : Kelley Astrid Ruud
language : en
Publisher:
Release Date : 1999
Identification And Characterization Of A Novel Cap Binding Protein From Arabidopsis Thaliana And Of The Wheat Eukaryotic Initiation Factor Eif4g written by Kelley Astrid Ruud and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1999 with Arabidopsis thaliana categories.
Chemical Abstracts
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Author :
language : en
Publisher:
Release Date : 2002
Chemical Abstracts written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2002 with Chemistry categories.
Identifying The Role Of The Cap Binding Complexes In The Regulation Of Translation In Arabidopsis Thaliana
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Author : Nicola Ann Cole
language : en
Publisher:
Release Date : 2017
Identifying The Role Of The Cap Binding Complexes In The Regulation Of Translation In Arabidopsis Thaliana written by Nicola Ann Cole and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2017 with categories.
There is a fundamental gap in our understanding of the regulation of translation in plants. None of the canonical eukaryotic methods found in mammals, such as the use of 4E-Binding protein phosphorylation and inhibition of eIF2B function by phosphorylation of eIF2[alpha], have been found in plants to date. In the very early steps of eukaryotic initiation of translation, the cap-binding complex, eIF4F, binds to the m7G of the mRNA and positions it for binding by the 43S preinitiation complex. This complex consists of the large scaffolding protein, eIF4G, and the smaller cap-binding protein, eIF4E, along with the DEAD box helicase eIF4A and the RNA binding protein eIF4B. In addition to eIF4F, plants have a well-conserved second cap-binding complex, eIFiso4F, not found in other eukaryotes and comprised of eIFiso4G and eIFiso4E, isoforms of the scaffolding protein and the cap-binding protein, respectively. Arabidopsis thaliana plants lacking eIFiso4F have stunted growth, reduced chlorophyll, reduced fertility and are more sensitive to light stress. In in vitro translation assays, there is a preference for eIF4F by capped messages. In this work, several possible methods for the regulation of translation in Arabidopsis thaliana by eIF4F and eIFiso4F are investigated. A previously discovered eIF4G wheat kinase known to phosphorylate eIF4G, eIFiso4G, eIF4B and a 60S ribosomal protein is further characterized to determine its possible role in the regulation of translation. It is found to be a calcium dependent kinase that phosphorylates eIFiso4G in the C-terminal domain most likely at a consensus sequence for calcium dependent protein kinases. Additionally, there is a conserved pair of cysteines located in the cap-binding pocket of both eIF4E and eIFiso4E, found only in plants. In an in vitro labeling assay, these cysteines are tested for their thiol reactivity in eIF4E versus eIFiso4E. eIFiso4E is found to be more thiol reactive than eIF4E, possibly indicating differences in redox activity between the two proteins. Finally, two methods for identifying specific populations of mRNA associated with plant protein synthesis initiation factors eIF4F and eIFiso4F are described, RNA immunoprecipitation and ribosome profiling.
Cumulated Index Medicus
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Author :
language : en
Publisher:
Release Date : 2000
Cumulated Index Medicus written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2000 with Medicine categories.
Evolution Of The Protein Synthesis Machinery And Its Regulation
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Author : Greco Hernández
language : en
Publisher: Springer
Release Date : 2016-08-10
Evolution Of The Protein Synthesis Machinery And Its Regulation written by Greco Hernández and has been published by Springer this book supported file pdf, txt, epub, kindle and other format this book has been release on 2016-08-10 with Science categories.
The “omics” era has given a new perspective to the findings on the origin and evolution of the process of translation. This book provides insight into the evolution of the translation process and machinery from a modern perspective. Written by leading experts in molecular biology, this text looks into the origins and evolution of the protein synthetic machinery.
American Doctoral Dissertations
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Author :
language : en
Publisher:
Release Date : 1999
American Doctoral Dissertations written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 1999 with Dissertation abstracts categories.
Dissertation Abstracts International
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Author :
language : en
Publisher:
Release Date : 2000
Dissertation Abstracts International written by and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2000 with Dissertations, Academic categories.
The Roles Of Alternative Cap Binding Proteins Of Arabidopsis Thaliana
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Author : Ryan Michael Patrick
language : en
Publisher:
Release Date : 2015
The Roles Of Alternative Cap Binding Proteins Of Arabidopsis Thaliana written by Ryan Michael Patrick and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2015 with categories.
The mRNA cap-binding complexes eIF4F (made up of the cap-binding protein eIF4E and the large scaffold eIF4G) and eIFiso4F (made up of the plant-specific isoforms eIFiso4E and eIFiso4G) have established roles in translation initiation. However, other cap-binding proteins are known to be encoded in the Arabidopsis thaliana genome. We have chosen to investigate the biochemical properties and potential functions of these proteins. We have identified the eIF4E-like proteins, eIF4E1b and eIF4E1c, as Brassicaceae-specific eIF4E isoforms with the ability to form cap-binding complexes. These proteins are able to complement an eIF4E deletion in yeast. However, their limited expression in A. thaliana along with their relatively weak binding affinity for eIF4G and more limited ability to promote translation in vitro indicate a possible role outside of canonical translation initiation pathways. The alternative cap-binding protein 4EHP is conserved from animals to plants, but its role and binding partners in plants are not well defined. We demonstrate that a homologous complex to the 4EHP-GIGYF2 cap-binding complex observed in mammals is present in A. thaliana. The plant complex appears important to proper development, as double knockouts show a noticeable developmental phenotype and dysregulation of gene expression, but the viability of these knockouts in A. thaliana may offer an opportunity to research the complex's function that cannot be performed in animal systems as knockouts are lethal. RNA immunoprecipitation studies find that 4EHP and GIGYF associate with non-coding RNA in A. thaliana, and nucleocytoplasmic fractionation supports a possible nuclear role for the proteins. These findings indicate that the 4EHP-GIGYF complex may have an unexpected role in bridging non-coding RNA to gene expression in plants.
Redox Control Of The Plant Specific Cap Binding Protein Eifiso4e In Arabidopsis
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Author : Ching-Ying Tseng (Ph. D.)
language : en
Publisher:
Release Date : 2015
Redox Control Of The Plant Specific Cap Binding Protein Eifiso4e In Arabidopsis written by Ching-Ying Tseng (Ph. D.) and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2015 with categories.
Eukaryotic initiation factor (eIF) 4E and the plant-specific homolog, eIFiso4E, participate in translation initiation by recognizing the 7‐methylguanosine (m7G) cap of mRNAs. All plant cap-binding proteins (eIF4E and eIFiso4E) have two conserved cysteine residues and wheat (Triticum aestivum) eIF4E was observed in crystals to form a disulfide bond between these two residues under oxidizing conditions. To study the effect of these conserved cysteines on Arabidopsis thaliana eIFiso4E activity in vivo or in vitro, one of the conserved residues (Cys-97) was mutated to serine (AteIFiso4E C97S), which abolishes the ability to form a disulfide bond or undergo modification. Under abiotic stress, AteIFiso4E C97S plants showed stress hypersensitivity and slowed ROS (reactive oxygen species) propagation, which suggests an in vivo role of Cys-97 in response to stress induced redox. The in vitro cap binding activity of AteIFiso4E C97S and in vitro translation activity of AteIFiso4F C97S (the complex of eIFiso4E C97S and eIFiso4G) was measured. AteIFiso4E C97S is not able to bind m7GTP-Sepharose affinity resin, but its binding can be restored by interaction with its binding partner, AteIFiso4G. However, a capped mRNA (barley [alpha]-amylase) was translated in vitro at a 3-fold lower rate by AteIFiso4F C97S compared to AteIFiso4F. These findings suggest that cysteine modification of AteIFiso4E and similarly conserved cysteine residues of other plant cap binding proteins (eIF4E) may have a role in regulation of translation during responses to the environment or other conditions that may alter the cellular redox status. To create a simple in vivo model for studying the differential activities of AteIF4E and AteIFiso4E or their complexes (AteIF4F and AteIFiso4F) towards messenger RNA (mRNA), yeast strains were created to attempt to substitute yeast eIF4E or eIF4G or both for Arabidopsis subunits. Lastly, an Arabidopsis mutant for ascorbic acid peroxidase (apx1) accumulates a high amount of cytosolic H2O2 which generates a more oxidizing environment. Arabidopsis carrying only exogenous AteIFiso4E or AteIFiso4E C97S in the eifiso4e/eif4e1/apx1 triple knockout were characterized for the response to this highly oxidizing environment.
Mismatch Repair In Plants
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Author : Kevin M. Culligan
language : en
Publisher:
Release Date : 2000
Mismatch Repair In Plants written by Kevin M. Culligan and has been published by this book supported file pdf, txt, epub, kindle and other format this book has been release on 2000 with Arabidopsis thaliana categories.
All eukaryotic organisms examined thus far encode homologs of the eubacterial DNA- mismatch-repair protein MutS. In comparison to other eukaryotic organisms, little is known about how plants combat mismatched DNA basepairs arising during the process of DNA replication. To address whether plants utilize similar MutS-homolog (MSH) proteins in mismatch-repair systems, I focused on three primary questions: i) Do plants encode homologs of MutS proteins? ii) Do these homologs fall into the same distinct subfamilies seen in other eukaryotes? iii) Do these homologs share conserved biochemical activities with their other eukaryotic counterparts? Using sets of degenerate polymerase chain reaction (PCR) primers corresponding to highly conserved MSH protein domains, I amplified and cloned segments of Arabidopsis thaliana cDNA. Two of these segments encoded conserved portions of Arabidopsis thaliana MSH genes, and their full-length cDNAs were isolated from Arabidopsis thaliana cDNA libraries. Utilizing Arabidopsis thaliana genome sequences deposited in GenBank, I further identified two other MSH genes; their full-length cDNAs were isolated from Arabidopsis thaliana mRNA using reverse-transcription (RT- ) PCR. Extensive phylogenetic analyses proved that the four predicted plant-protein sequences clearly fell into the conserved MSH2, MSH3 and MSH6 sub-families seen in other eukaryotes. Furthermore, the phylogenetic analyses revealed a novel feature in higher plants the presence of two MSH6-like proteins, designated MSH6 and MSH7. Combinations of Arabidopsis thaliana atMSH2, atMSH3, atMSH6, and atMSH7 proteins, products of in vitro transcription and translation, were analyzed for protein-protein interactions. The atMSH2 protein formed heterodimers with atMSH6, atMSH3, or atMSH7 proteins (designated atMutS[Alpha], atMutS[Beta], and atMutS[Gamma], respectively) but no other complexes were observed. The abilities of the various heterodimers to bind to mismatched 51-mer oligoduplexes were measured by electrophoretic mobility-shift assays. Both atMutS[Alpha] and atMutS[Beta] shared conserved mismatch specificities with their eukaryotic counterparts, but MutS[Gamma] showed a novel substrate specificity. These data suggest that plants utilize unique mismatch-repair pathways to maintain the integrity of their genomes.