RNA-Binding Protein RBP-P Is Required for Glutelin and Prolamine mRNA Localization in Rice Endosperm Cells

Tian, Li; Chou, Hong Li; Zhang, Laining; Hwang, Seon‐Kap; Starkenburg, Shawn R.; Doroshenk, Kelly A.; Kumamaru, Toshihiro; Okita, Thomas W.

doi:10.1105/tpc.18.00321

Cited by 49 publications

(72 citation statements)

References 72 publications

(128 reference statements)

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“…The interrelatedness of the three RNA transport pathways suggests that they share common trans-factors for targeting to the ER membrane, while glutelin and prolamine pathways require additional factors for selective transport (Chou et al, 2019). Indeed, our studies showed that prolamine and glutelin zipcode sequences bind identical transfactors, Tudor-SN (Chou et al, 2017;Tian et al, 2018, 2019), RBP-P (Chou et al, 2017; Tian et al, 2018, 2019), and RBP-L (Chou et al, 2017;Tian et al, 2018Tian et al, , 2019.…”

Section: Mrna Localization In Plant Cellsmentioning

confidence: 65%

“…RBP-P contains two RRMs flanked by Ala/Glu-rich N-terminal and Gly-rich C-terminal domains. The two RRMs in RBP-P directly contribute to its strong binding to glutelin and prolamine mRNAs (Tian et al, 2018). The auxiliary domains flanking the RRMs, especially the Gly-rich region, mediated both RNA binding and protein-protein interaction (Tian et al, 2018).…”

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

“…The two RRMs in RBP-P directly contribute to its strong binding to glutelin and prolamine mRNAs (Tian et al, 2018). The auxiliary domains flanking the RRMs, especially the Gly-rich region, mediated both RNA binding and protein-protein interaction (Tian et al, 2018). Point mutations in the interdomain (A252T) that separated the two RRM motifs and the C-terminal Gly-rich region (G373E and G401S) reduced the association of RBP-P with prolamine and glutelin mRNAs in vivo and caused mislocalization of these mRNAs (Tian et al, 2018), suggesting an essential role of RBP-P in mRNA localization.…”

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

“…The role of RBP-P in glutelin and prolamine mRNA localization also requires its association with other RBPs to form one or more multiprotein complexes. A yeast two-hybrid screening analysis of a rice seed cDNA library identified two major interacting partners, RBP-L and RBP208 (Tian et al, 2018). These RBPs, which contain three RRM motifs, coassembled with RBP-P into multiprotein complexes that specifically bind to prolamine and glutelin zipcode RNAs, as revealed by in vivo RNA-immunoprecipitation studies (Tian et al, 2018).…”

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

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mRNA Localization in Plant Cells

et al. 2019

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Localization of mRNAs at the subcellular level is an essential mechanism for specific protein targeting and local control of protein synthesis in both eukaryotes and bacteria. While mRNA localization is well documented in metazoans, somatic cells, and microorganisms, only a handful of well-defined mRNA localization examples have been reported in vascular plants and algae. This review summarizes the function and mechanism of mRNA localization and highlights recent studies of mRNA localization in vascular plants. While the emphasis focuses on storage protein mRNA localization in rice endosperm cells, information on targeting of RNAs to organelles (chloroplasts and mitochondria) and plasmodesmata is also discussed. WHAT IS MRNA LOCALIZATION? Localization of mRNAs was initially discovered in the 1980s, when b-actin mRNA was found to be asymmetrically distributed in ascidian eggs and embryos (Jeffery et al., 1983). This nonuniform spatial distribution pattern was later observed for maternal mRNAs in Xenopus (Rebagliati et al., 1985) and Drosophila oocytes (Frigerio et al., 1986; Berleth et al., 1988) and supported the proposal of prelocalized RNA during early development (Davidson, 1971; Kandler-Singer and Kalthoff, 1976). Subsequently, mRNA localization was observed in a variety of somatic cells such as fibroblasts (Lawrence and Singer, 1986), oligodendrocytes (Trapp et al., 1997), and neurons (Garner et al., 1988). Today, mRNA localization is prevalent in bacteria, yeast, algae, vascular plants, and metazoans and, therefore, is an ancient, universal, evolutionarily conserved mechanism. Our understanding of mRNA localization stems mainly from research in Xenopus, Drosophila, budding yeast, fungi, and structurally polarized animal cells

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Section: Mrna Localization In Plant Cellsmentioning

confidence: 65%

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

Section: Identification Of Trans-factors That Recognize Storage Protementioning

confidence: 99%

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mRNA Localization in Plant Cells

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“…Transmission electron microscopy (TEM) analysis was performed as previously described (Tian and Sun 2011;Tian et al, 2018).…”

Section: Microscopy Analysismentioning

confidence: 99%

Re‐programming of gene expression in the CS8 rice line over‐expressing ADPglucose pyrophosphorylase induces a suppressor of starch biosynthesis

et al. 2019

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Summary The CS8 transgenic rice (Oryza sativa L.) lines expressing an up‐regulated glgC gene produced higher levels of ADPglucose (ADPglc), the substrate for starch synthases. However, the increase in grain weight was much less than the increase in ADPglc levels suggesting one or more downstream rate‐limiting steps. Endosperm starch levels were not further enhanced in double transgenic plants expressing both glgC and the maize brittle‐1 gene, the latter responsible for transport of ADPglc into the amyloplast. These studies demonstrate that critical processes within the amyloplast stroma restrict maximum carbon flow into starch. RNA‐seq analysis showed extensive re‐programming of gene expression in the CS8 with 2073 genes up‐regulated and 140 down‐regulated. One conspicuous gene, up‐regulated ~15‐fold, coded for a biochemically uncharacterized starch binding domain‐containing protein (SBDCP1) possessing a plastid transit peptide. Confocal microscopy and transmission electron microscopy analysis confirmed that SBDCP1 was located in the amyloplasts. Reciprocal immunoprecipitation and pull‐down assays indicated an interaction between SBDCP1 and starch synthase IIIa (SSIIIa), which was down‐regulated at the protein level in the CS8 line. Furthermore, binding by SBDCP1 inhibited SSIIIa starch polymerization activity in a non‐competitive manner. Surprisingly, artificial microRNA gene suppression of SBDCP1 restored protein expression levels of SSIIIa in the CS8 line resulting in starch with lower amylose content and increased amylopectin chains with a higher degree of polymerization. Collectively, our results support the involvement of additional non‐enzymatic factors such as SBDCP in starch biosynthesis.

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Seed-Based Production System for Molecular Farming

Takaiwa

2023

Concepts and Strategies in Plant Sciences

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RNA-Binding Protein RBP-P Is Required for Glutelin and Prolamine mRNA Localization in Rice Endosperm Cells

Cited by 49 publications

References 72 publications

mRNA Localization in Plant Cells

mRNA Localization in Plant Cells

Re‐programming of gene expression in the CS8 rice line over‐expressing ADPglucose pyrophosphorylase induces a suppressor of starch biosynthesis

Seed-Based Production System for Molecular Farming

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