Identification of Polypeptides Associated with an Enriched Cytoskeleton-Protein Body Fraction from Developing Rice Endosperm

Wu, Yujia; Muench, Douglas G.; Kim, Yeong-Tae; Hwang, Young-Soo; Okita, Thomas W.

doi:10.1093/oxfordjournals.pcp.a029328

Cited by 11 publications

(14 citation statements)

References 58 publications

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“…3). Proteins that function in translation have been reported to bind to the cytoskeleton (21,42), and several of these proteins were identified here, including translation initiation and elongation factors, aminoacyl-tRNA synthetases, and ribosomal proteins. This concentration of the translational machinery on the cytoskeleton may function to increase the efficiency of translation, or serve as a mechanism to regulate translation rate (42).…”

Section: Discussionmentioning

confidence: 91%

“…Gel Electrophoresis-SDS-PAGE, two-dimensional NEPHGE, and immunoblot analysis were performed as described previously (5,21). Protein gels were stained with either Coomassie Brilliant Blue stain (R-250) or by silver staining (Silver Stain Plus; Bio-Rad, Hercules, CA).…”

Section: Methodsmentioning

confidence: 99%

“…These types of studies have also been performed in plants. Using a detergent-resistant cytoskeleton/ protein body fraction from rice and maize endosperm cells, 15 and 5 cytoskeleton-associated proteins were identified, respectively (21,22). Another plant study identified 8 proteins from a detergent-resistant protein fraction from pea stems (12).…”

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confidence: 99%

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Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Chuong

Good

Taylor

et al. 2004

Molecular & Cellular Proteomics

115

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Microtubules play an essential role in the growth and development of plants and are known to be involved in regulating many cellular processes ranging from translation to signaling. In this article, we describe the proteomic characterization of Arabidopsis tubulin-binding proteins that were purified using tubulin affinity chromatography. Microtubule co-sedimentation assays indicated that most, if not all, of the proteins in the tubulin-binding protein fraction possessed microtubule-binding activity. Two-dimensional gel electrophoresis of the tubulin-binding protein fraction was performed, and 86 protein spots were excised and analyzed for protein identification. A total of 122 proteins were identified with high confidence using LC-MS/MS. These proteins were grouped into six categories based on their predicted functions: microtubule-associated proteins, translation factors, RNA-binding proteins, signaling proteins, metabolic enzymes, and proteins with other functions. Almost one-half of the proteins identified in this fraction were related to proteins that have previously been reported to interact with microtubules. This study represents the first large-scale proteomic identification of eukaryotic cytoskeleton-binding proteins, and provides insight on subcellular trafficking, metabolic channeling, and signaling in plant cells. Molecular & Cellular Proteomics 3:970 -983, 2004.The cytoskeleton is the single most important structure that contributes to the highly ordered organization of the eukaryotic cell. It provides a framework for cell division and the trafficking of organelles and macromolecules, and also serves to regulate important cellular processes such as signaling, translation, and metabolism. The cytoskeleton plays a key role in a number of plant-specific processes, such as assisting in the formation of the cell plate, regulating cell-to-cell movement, and influencing the direction of cell elongation (1). A role for the microtubule (MT) 1 component of the cytoskeleton in many of these processes has been demonstrated, and a number of MT-binding proteins that are responsible for regulating these events have been identified.Plant MTs are assembled into four distinct arrays during the cell cycle (2). Three of these arrays-the interphase cortical array, the pre-prophase band, and the phragmoplast-have no counterpart in animal cells. The cortical MT array has been linked to the regulation of cellulose microfibril deposition and, hence, a role in cell expansion, while the pre-prophase band and the phragmoplast have important roles in the positioning and synthesis of the new cell plate in dividing cells. The fourth array, the spindle, has an evolutionarily conserved role in the segregation of chromosomes during cell division. The organization and dynamics of MTs in these arrays depend on the activity of various MT-associated proteins (MAPs). Several plant MAPs have been identified, including the 65-kDa MAPs, MAP 190, and MOR1 (3). These proteins are important in cross-bridging MTs, linking MTs with actin filamen...

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Section: Discussionmentioning

confidence: 91%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Chuong

Good

Taylor

et al. 2004

Molecular & Cellular Proteomics

115

View full text Add to dashboard Cite

show abstract

“…Gel Electrophoresis, Protein Gel Blot Analysis, and Antiserum Production-SDS-PAGE, two-dimensional non-equilibrium pH gel electrophoresis (NEPHGE), and protein gel blot analysis were carried out as described previously (37). For protein gel blots, rice MFP and elongation factor-1␣ (EF-1␣) antisera were both used at a dilution of 1:500, and horseradish peroxidase-conjugated anti-rabbit secondary antibodies (Sigma) were used at a dilution of 1:3000.…”

Section: Methodsmentioning

confidence: 99%

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

Chuong¹,

Mullen²,

Muench³

2002

Journal of Biological Chemistry

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The control of subcellular mRNA localization and translation is often mediated by protein factors that are directly or indirectly associated with the cytoskeleton. We report the identification and characterization of a rice seed protein that possesses both RNA and microtubule binding activities. In vitro UV cross-linking assays indicated that this protein binds to all mRNA sequences tested, although there was evidence for preferential binding to RNAs that contained A-C nucleotide sequence motifs. The protein was purified to homogeneity using a two-step procedure, and amino acid sequencing identified it as the multifunctional protein (MFP), a peroxisomal enzyme known to possess a number of activities involved in the ␤-oxidation of fatty acids. The recombinant version of this rice MFP binds to RNA in UV cross-linking and gel mobility shift experiments, co-sediments specifically with microtubules, and possesses at least two enzymatic activities involved in peroxisomal fatty acid ␤-oxidation. Taken together these data suggest that MFP has an important role in mRNA physiology in the cytoplasm, perhaps in regulating the localization or translation of mRNAs through an interaction with microtubules, in addition to its peroxisomal function.

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“…, 1992) and is one of the most highly expressed genes during rice endosperm development (Krishnan et al. , 1992; Wu et al. , 1998).…”

Section: Introductionmentioning

confidence: 99%

RNA targeting to a specific ER sub‐domain is required for efficient transport and packaging of α‐globulins to the protein storage vacuole in developing rice endosperm

et al. 2012

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SUMMARYStudies focusing on the targeting of RNAs that encode rice storage proteins, prolamines and glutelins to specific sub-domains of the endoplasmic reticulum (ER), as well as mis-localization studies of other storage protein RNAs, indicate a close relationship between the ER site of RNA translation and the final site of protein deposition in the endomembrane system in developing rice endosperm. In addition to prolamine and glutelin, rice accumulates smaller amounts of a-globulins, which are deposited together with glutelin in the protein storage vacuole (PSV). In situ RT-PCR analysis revealed that a-globulin RNAs are not distributed to the cisternal ER as expected for a PSV-localized protein, but instead are targeted to the protein body-ER (PB-ER) by a regulated process requiring cis-sorting sequences. Sequence alignments with putative maize d-zein cis-localization elements identified several candidate regulatory sequences that may be responsible for PB-ER targeting. Immunocytochemical analysis confirmed the presence of a-globulin on the periphery of the prolamine protein bodies and packaging in Golgi-associated dense vesicles, as well as deposition and storage within peripheral regions of the PSV. Mis-targeting of a-globulin RNAs to the cisternal ER dramatically alters the spatial arrangement of a-globulin and glutelin within the PSV, with the accompanying presence of numerous small a-globulin particles in the cytoplasm. These results indicate that a-globulin RNA targeting to the PB-ER sub-domain is essential for efficient transport of a-globulins to the PSV and its spatial arrangement in the PSV. Such RNA localization prevents potential deleterious protein-protein interactions, in addition to performing a role in protein targeting.

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Identification of Polypeptides Associated with an Enriched Cytoskeleton-Protein Body Fraction from Developing Rice Endosperm

Cited by 11 publications

References 58 publications

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Identification of a Rice RNA- and Microtubule-binding Protein as the Multifunctional Protein, a Peroxisomal Enzyme Involved in the β-Oxidation of Fatty Acids

RNA targeting to a specific ER sub‐domain is required for efficient transport and packaging of α‐globulins to the protein storage vacuole in developing rice endosperm

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