Database : MEDLINE Search on : Arabidopsis and Proteins [Words] References found : 42456 [refine] Displaying: 1 .. 10   in format [Detailed]

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[PMID]: 29524407 [Au] Autor: Yu CY; Nguyen VC; Chuang L; Kanehara K [Ad] Address: Institute of Plant and Microbial Biology, Academia Sinica, Taipei 11529, Taiwan; Molecular and Biological Agricultural Sciences Program, Taiwan International Graduate Program, Academia Sinica and National Chung Hsing University, Taipei 11529, Taiwan; Graduate Institute of Biotechnology, National Chu [Ti] Title: Membrane glycerolipid equilibrium under endoplasmic reticulum stress in Arabidopsis thaliana. [So] Source: Biochem Biophys Res Commun;, 2018 Mar 07. [Is] ISSN: 1090-2104 [Cp] Country of publication: United States [La] Language: eng [Ab] Abstract: Eendoplasmic reticulum (ER) is an indispensable organelle for secretory protein synthesis as well as metabolism of phospholipids and their derivatives in eukaryotic cells. Various external and internal factors may cause an accumulation of aberrant proteins in the ER, which causes ER stress and activates cellular ER stress responses to cope with the stress. In animal research, molecular mechanisms for protein quality control upon ER stress are well documented, but how cells maintain lipid homeostasis under ER stress is an emerging issue. The ratio of phosphatidylcholine (PC) to phosphatidylethanolamine (PE), two major phospholipid classes, is important under ER stress in animal cells. However, no study of plants has reported on the changes in membrane lipid content under ER stress, although a number of physiologically important environmental stresses, such as heat and salinity, induce ER stress in plants. Here, we investigated membrane glycerolipid metabolism under ER stress in Arabidopsis. ER stress transcriptionally affected PC and PE biosynthesis pathways differentially, with no significant changes in membrane glycerolipid content. Our results suggest that higher plants maintain membrane lipid equilibrium during active transcription of biosynthetic genes under ER stress. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher

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[PMID]: 29499229 [Au] Autor: Chumová J; Trögelová L; Kourová H; Volc J; Sulimenko V; Halada P; Kucera O; Benada O; Kucharová A; Klebanovych A; Dráber P; Daniel G; Binarová P [Ad] Address: Institute of Microbiology of the Czech Academy of Sciences, Vídenská 1083, 142 20 Prague 4, Czech Republic. [Ti] Title: γ-Tubulin has a conserved intrinsic property of self-polymerization into double stranded filaments and fibrillar networks. [So] Source: Biochim Biophys Acta;1865(5):734-748, 2018 Feb 27. [Is] ISSN: 0006-3002 [Cp] Country of publication: Netherlands [La] Language: eng [Ab] Abstract: γ-Tubulin is essential for microtubule nucleation and also plays less understood roles in nuclear and cell-cycle-related functions. High abundancy of γ-tubulin in acentrosomal Arabidopsis cells facilitated purification and biochemical characterization of large molecular species of γ-tubulin. TEM, fluorescence, and atomic force microscopy of purified high molecular γ-tubulin forms revealed the presence of linear filaments with a double protofilament substructure, filament bundles and aggregates. Filament formation from highly purified γ-tubulin free of γ-tubulin complex proteins (GCPs) was demonstrated for both plant and human γ-tubulin. Moreover, γ-tubulin associated with porcine brain microtubules formed oligomers. Experimental evidence on the intrinsic ability of γ-tubulin to oligomerize/polymerize was supported by conservation of α- and ß-tubulin interfaces for longitudinal and lateral interactions for γ-tubulins. STED (stimulated emission depletion) microscopy of Arabidopsis cells revealed fine, short γ-tubulin fibrillar structures enriched on mitotic microtubular arrays that accumulated at polar regions of acentrosomal spindles and the outer nuclear envelope before mitosis, and were also present in nuclei. Fine fibrillar structures of γ-tubulin representing assemblies of higher order were localized in cell-cycle-dependent manner at sites of dispersed γ-tubulin location in acentrosomal plant cells as well as at sites of local γ-tubulin enrichment after drug treatment. Our findings that γ-tubulin preserves the capability of prokaryotic tubulins to self-organize into filaments assembling by lateral interaction into bundles/clusters help understanding of the relationship between structure and multiple cellular functions of this protein species and suggest that besides microtubule nucleation and organization, γ-tubulin may also have scaffolding or sequestration functions. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher

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[PMID]: 29482161 [Au] Autor: Yang Q; Wang L; He J; Yang Z; Huang X [Ad] Address: National and Local Joint Engineering Research Center of Biomedical Functional Materials, Jiangsu Collaborative Innovation Center of Biomedical Functional Materials, School of Chemistry and Materials Sciences, Nanjing Normal University, Nanjing 210046, China. [Ti] Title: Direct imaging of how lanthanides break the normal evolution of plants. [So] Source: J Inorg Biochem;182:158-169, 2018 Feb 10. [Is] ISSN: 1873-3344 [Cp] Country of publication: United States [La] Language: eng [Ab] Abstract: After rare earth elements [REE(III)] are anchored outside of the plasma membrane, REE(III) break plant evolution to initiate leaf cell endocytosis, which finally affects plant growth. However, the molecule for anchoring REE(III) in the acidic environment outside of the plasma membrane is not clear, which is crucial for exploring the mechanism of REE(III) breaking plant evolution. Here, lanthanum(III) [La(III)] and terbium(III) [Tb(III)] were respectively served as a representative of REE(III) without and with f electrons, and Arabidopsis was served as a representative of plants, cellular and molecular basis for arabinogalactan proteins (AGP) anchoring REE(III) outside of the plasma membrane was investigated. By using interdisciplinary methods, when REE(III) initiated leaf cell phagocytosis, we observed the increase in the expression of AGP and their migration to the outside of the plasma membrane. In the acidic environment outside of the plasma membrane, Tb(III) formed more stable Lewis acid-base [REE(III)-AGP] complexes with a higher apparent binding constant (1.51 × 10 ) than La(III) (1.24 × 10 ). In REE(III)-AGP complexes, the bond lengths of REE(III)-O were in normal range and H-bonds were strong H-bonds. The formation of REE(III)-AGP complexes sequentially disturbed the secondary and tertiary structure of AGP, which were enhanced with increasing the concentration of REE(III), and Tb(III) caused stronger structural changes than La(III). Hence, AGP could be molecules for anchoring REE(III) outside of the plasma membrane. The results of this study are direct imaging of how lanthanides break the normal evolution of plants, and can serve as an important guidance for investigating mechanism of lanthanides in organisms. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1802 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher

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[PMID]: 29523961 [Au] Autor: Peng F; Wang C; Zhu J; Zeng J; Kang H; Fan X; Sha L; Zhang H; Zhou Y; Wang Y [Ad] Address: Triticeae Research Institute, Sichuan Agricultural University, Wenjiang, 611130, Sichuan, China. [Ti] Title: Expression of TpNRAMP5, a metal transporter from Polish wheat (Triticum polonicum L.), enhances the accumulation of Cd, Co and Mn in transgenic Arabidopsis plants. [So] Source: Planta;, 2018 Mar 09. [Is] ISSN: 1432-2048 [Cp] Country of publication: Germany [La] Language: eng [Ab] Abstract: MAIN CONCLUSION: TpRNAMP5 is mainly expressed in the plasma membrane of roots and basal stems. It functions as a metal transporter for Cd, Mn and Co accumulation. Numerous natural resistance-associated macrophage proteins (NRAMPs) have been functionally identified in various plant species, including Arabidopsis, rice, soybean and tobacco, but no information is available on NRAMP genes in wheat. In this study, we isolated a TpNRAMP5 from dwarf Polish wheat (DPW, Triticum polonicum L.), a species with high tolerance to Cd and Zn. Expression pattern analysis revealed that TpNRAMP5 is mainly expressed in roots and basal stems of DPW. TpNRAMP5 was localized at the plasma membrane of Arabidopsis leaf protoplast. Expression of TpNRAMP5 in yeast significantly increased yeast sensitivity to Cd and Co, but not Zn, and enhanced Cd and Co concentrations. Expression of TpNRAMP5 in Arabidopsis significantly increased Cd, Co and Mn concentrations in roots, shoots and whole plants, but had no effect on Fe and Zn concentrations. These results indicate that TpNRAMP5 is a metal transporter enhancing the accumulation of Cd, Co and Mn, but not Zn and Fe. Genetic manipulation of TpNRAMP5 can be applied in the future to limit the transfer of Cd from soil to wheat grains, thereby protecting human health. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher [do] DOI: 10.1007/s00425-018-2872-3

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[PMID]: 29523715 [Au] Autor: Kumar M; Mishra L; Carr P; Pilling M; Gardner P; Mansfield SD; Turner SR [Ad] Address: University of Manchester CITY: Manchester United Kingdom [GB]. [Ti] Title: Exploiting CELLULOSE SYNTHASE (CESA) class-specificity to probe cellulose microfibril biosynthesis. [So] Source: Plant Physiol;, 2018 Mar 09. [Is] ISSN: 1532-2548 [Cp] Country of publication: United States [La] Language: eng [Ab] Abstract: Cellulose microfibrils are the basic units of cellulose in plants. The structure of these microfibrils is at least partly determined by the structure of the cellulose synthase complex. In higher plants, this complex is composed of 18 to 24 catalytic subunits known as CELLULOSE SYNTHASE A (CESA) proteins. Three different classes of CESA proteins are required for cellulose synthesis and for secondary cell wall cellulose biosynthesis, which include CESA4, CESA7, and CESA8. To probe the relationship between CESA proteins and microfibril structure, we created mutant cesa proteins that lack catalytic activity but retain sufficient structural integrity to allow assembly of the cellulose synthase complex. Using a series of Arabidopsis mutants and genetic backgrounds, we found consistent differences in the ability of these mutant CESA proteins to complement the cellulose-deficient phenotype of the cesa null mutants. The best complementation was observed with catalytically inactive cesa4 while the equivalent mutation in cesa8 exhibited significantly lower levels of complementation. Using a variety of biophysical techniques, including ssNMR and FTIR, to study these mutant plants we found evidence for changes in cellulose microfibril structure, but these changes largely correlated with cellulose content and reflected differences in the relative proportion of primary and secondary cell walls. Our results suggest that individual CESA classes have similar roles in determining cellulose microfibril structure, and it is likely that the different effects of mutating members of different CESA classes is a consequence of their different catalytic activity and their influence on the overall rate of cellulose synthesis. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher

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[PMID]: 29523712 [Au] Autor: Feng QN; Liang X; Li S; Zhang Y [Ad] Address: State Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University CITY: Tai'an China [CN]. [Ti] Title: The ADAPTOR PROTEIN-3 complex mediates pollen tube growth by coordinating vacuolar targeting and organization. [So] Source: Plant Physiol;, 2018 Mar 09. [Is] ISSN: 1532-2548 [Cp] Country of publication: United States [La] Language: eng [Ab] Abstract: Pollen tube growth is an essential step for successful plant reproduction. Vacuolar trafficking and dynamic organization are important for pollen tube growth; however, the key proteins involved in these processes are not well understood. Here, we report that the ADAPTOR PROTEIN-3 (AP-3) complex and its tonoplast cargo PROTEIN S-ACYL TRANSFERASE10 (PAT10) are critical for pollen tube growth in Arabidopsis (Arabidopsis thaliana). AP-3 is a heterotetrameric protein complex consisting of four subunits, δ, ß, µ, and σ. AP-3 regulates tonoplast targeting of several cargoes, such as PAT10. We show that functional loss of any of the four AP-3 subunits reduces plant fertility. In ap-3 mutants, pollen development was normal but pollen tube growth was compromised, leading to reduced male transmission. Functional loss of PAT10 caused a similar reduction in pollen tube growth, suggesting that the tonoplast association of PAT10 mediated by AP-3 is crucial for this process. Indeed, Ca2+ gradient during pollen tube growth was significantly reduced due to AP-3 loss-of-function, consistent with the abnormal targeting of Calcinuerin B-like2 (CBL2) and CBL3, whose tonoplast association depends on PAT10. Further, we show that the pollen tubes of ap-3 mutants have vacuoles with simplified tubules and bulbous structures, indicating that AP-3 affects vacuolar organization. Our results demonstrate a role for AP-3 in plant reproduction and provide insights into the role of vacuoles in polarized cell growth. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher

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[PMID]: 29522990 [Au] Autor: Trasviña-Arenas CH; Baruch-Torres N; Cordoba-Andrade FJ; Ayala-García VM; García-Medel PL; Díaz-Quezada C; Peralta-Castro A; Ordaz-Ortiz JJ; Brieba LG [Ad] Address: Langebio-Cinvestav Sede Irapuato, Km. 9.6 Libramiento Norte Carretera, Irapuato-León, 36821 Irapuato, Guanajuato, Mexico. [Ti] Title: Identification of a unique insertion in plant organellar DNA polymerases responsible for 5'-dRP lyase and strand-displacement activities: Implications for Base Excision Repair. [So] Source: DNA Repair (Amst);65:1-10, 2018 Feb 27. [Is] ISSN: 1568-7856 [Cp] Country of publication: Netherlands [La] Language: eng [Ab] Abstract: Plant mitochondrial and chloroplast genomes encode essential proteins for oxidative phosphorylation and photosynthesis. For proper cellular function, plant organelles must ensure genome integrity. Although plant organelles repair damaged DNA using the multi-enzyme Base Excision Repair (BER) pathway, the details of this pathway in plant organelles are largely unknown. The initial enzymatic steps in BER produce a 5'-deoxyribose phosphate (5'-dRP) moiety that must be removed to allow DNA ligation and in plant organelles, the enzymes responsible for the removal of a 5'-dRP group are unknown. In metazoans, DNA polymerases (DNAPs) remove the 5'-dRP moiety using their intrinsic lyase and/or strand-displacement activities during short or long-patch BER sub-pathways, respectively. The plant model Arabidopsis thaliana encodes two family-A DNAPs paralogs, AtPolIA and AtPolIB, which are the sole DNAPs in plant organelles identified to date. Herein we demonstrate that both AtPolIs present 5'-dRP lyase activities. AtPolIB performs efficient strand-displacement on a BER-associated 1-nt gap DNA substrate, whereas AtPolIA exhibits only moderate strand-displacement activity. Both lyase and strand-displacement activities are dependent on an amino acid insertion that is exclusively present in plant organellar DNAPs. Within this insertion, we identified that residue AtPollB-Lys593 acts as nucleophile for lyase activity. Our results demonstrate that AtPolIs are functionally equipped to play a role in short-patch BER and suggest a major role of AtPolIB in a predicted long-patch BER sub-pathway. We propose that the acquisition of insertion 1 in the polymerization domain of AtPolIs was a key component in their evolution as BER associated and replicative DNAPs. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180309 [Lr] Last revision date: 180309 [St] Status: Publisher

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[PMID]: 29522510 [Au] Autor: Sun Z; Li M; Zhou Y; Guo T; Liu Y; Zhang H; Fang Y [Ad] Address: National key Laboratory of Plant Molecular Genetics, CAS Center for Excellence in Molecular Plant Sciences, Institute of Plant Physiology and Ecology, Chinese Academy of Sciences, Shanghai, China; University of the Chinese Academy of Sciences, Beijing, China. [Ti] Title: Coordinated regulation of Arabidopsis microRNA biogenesis and red light signaling through Dicer-like 1 and phytochrome-interacting factor 4. [So] Source: PLoS Genet;14(3):e1007247, 2018 Mar 09. [Is] ISSN: 1553-7404 [Cp] Country of publication: United States [La] Language: eng [Ab] Abstract: Light and microRNAs (miRNAs) are key external and internal signals for plant development, respectively. However, the relationship between the light signaling and miRNA biogenesis pathways remains unknown. Here we found that miRNA processer proteins DCL1 and HYL1 interact with a basic helix-loop-helix (bHLH) transcription factor, phytochrome-interacting factor 4 (PIF4), which mediates the destabilization of DCL1 during dark-to-red-light transition. PIF4 acts as a transcription factor for some miRNA genes and is necessary for the proper accumulation of miRNAs. DCL1, HYL1, and mature miRNAs play roles in the regulation of plant hypocotyl growth. These results uncovered a previously unknown crosstalk between miRNA biogenesis and red light signaling through the PIF4-dependent regulation of miRNA transcription and processing to affect red-light-directed plant photomorphogenesis. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1803 [Cu] Class update date: 180309 [Lr] Last revision date: 180309 [St] Status: Publisher [do] DOI: 10.1371/journal.pgen.1007247

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[PMID]: 29385650 [Au] Autor: Lin S; Yue X; Miao Y; Yu Y; Dong H; Huang L; Cao J [Ad] Address: Laboratory of Cell & Molecular Biology, Institute of Vegetable Science, Zhejiang University, Hangzhou, 310058, China. [Ti] Title: The distinct functions of two classical arabinogalactan proteins BcMF8 and BcMF18 during pollen wall development in Brassica campestris. [So] Source: Plant J;, 2018 Jan 31. [Is] ISSN: 1365-313X [Cp] Country of publication: England [La] Language: eng [Ab] Abstract: Arabinogalactan proteins (AGPs) are extensively glycosylated hydroxyproline-rich glycoproteins ubiquitous in all plant tissues and cells. AtAGP6 and AtAGP11, the only two functionally known pollen-specific classical AGP encoding genes in Arabidopsis, are reported to have redundant functions in microspore development. BcMF18 and BcMF8 isolated from Brassica campestris are the orthologues of AtAGP6 and AtAGP11, respectively. In contrast to the functional redundancy of AtAGP6 and AtAGP11, single-gene disruption of BcMF8 led to deformed pollen grains with abnormal intine development and ectopic aperture formation in B. campestris. Here, we further explored the action of BcMF18 and its relationship with BcMF8. BcMF18 was specifically expressed in pollen during the late stages of microspore development. Antisense RNA transgenic lines with BcMF18 reduction resulted in aberrant pollen grains with abnormal cellulose distribution, lacking intine, cytoplasm and nuclei. Transgenic plants with repressive expression of both BcMF8 and BcMF18 showed a hybrid phenotype, expressing a mixture of the phenotypes of the single gene knockdown plant lines. In addition, we identified functional diversity between BcMF18/BcMF8 and AtAGP6/AtAGP11, mainly reflected by the specific contribution of BcMF18 and BcMF8 to pollen wall formation. These results suggest that, unlike the orthologous genes AtAGP6 and AtAGP11 in Arabidopsis, BcMF18 and BcMF8 are both integral to pollen biogenesis in B. campestris, acting through independent pathways during microspore development. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1802 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher [do] DOI: 10.1111/tpj.13842

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[PMID]: 29385648 [Au] Autor: Otani T; Kato Y; Shikanai T [Ad] Address: Department of Botany, Graduate School of Science, Kyoto University, Kyoto, 606-8502, Japan. [Ti] Title: Specific substitutions of light-harvesting complex I proteins associated with photosystem I are required for supercomplex formation with chloroplast NADH dehydrogenase-like complex. [So] Source: Plant J;, 2018 Jan 31. [Is] ISSN: 1365-313X [Cp] Country of publication: England [La] Language: eng [Ab] Abstract: In Arabidopsis, the chloroplast NADH-dehydrogenase-like (NDH) complex is sandwiched between two copies of photosystem I (PSI) supercomplex, consisting of a PSI core and four light-harvesting complex I (LHCI) proteins (PSI-LHCI) to form the NDH-PSI supercomplex. Two minor LHCI proteins, Lhca5 and Lhca6, contribute to the interaction of each PSI-LHCI copy with the NDH complex. Here, large-pore blue-native gel electrophoresis revealed that, in addition to this complex, there were at least two types of higher-order association of more LHCI copies with the NDH complex. In single-particle images, this higher-order association of PSI-LHCI preferentially occurs at the left side of the NDH complex when viewed from the stromal side, placing subcomplex A at the top (Yadav et al., Biochim. Biophys. Acta - Bioenerg., 1858, 2017, 12). The association was impaired in the lhca6 mutant but not in the lhca5 mutant, suggesting that the left copy of PSI-LHCI was linked to the NDH complex via Lhca6. From an analysis of subunit compositions of the NDH-PSI supercomplex in lhca5 and lhca6 mutants, we propose that Lhca6 substitutes for Lhca2 in the left copy of PSI-LHCI, whereas Lhca5 substitutes for Lhca4 in the right copy. In the lhca2 mutant, Lhca3 was specifically stabilized in the NDH-PSI supercomplex through heterodimer formation with Lhca6. In the left copy of PSI-LHCI, subcomplex B, Lhca6 and NdhD likely formed the core of the supercomplex interaction. In contrast, a larger protein complex, including at least subcomplexes B and L and NdhB, was needed to form the contact site with Lhca5 in the right copy of PSI-LHCI. [Pt] Publication type: JOURNAL ARTICLE [Em] Entry month: 1802 [Cu] Class update date: 180310 [Lr] Last revision date: 180310 [St] Status: Publisher [do] DOI: 10.1111/tpj.13846

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