A Role for the Cysteine-Rich 10 kDa Prolamin in Protein Body I Formation in Rice

Nagamine, Ai; Matsusaka, Hiroaki; Ushijima, Tomokazu; Kawagoe, Yasuhiro; Ogawa, Masahiro; Okita, Thomas W.; Kumamaru, Toshihiro

doi:10.1093/pcp/pcr053

Cited by 61 publications

(56 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In this study, however, globulin-less mutation was unique to induce partial degradation of glutelin rather than compensation. Although compositional change of protein bodies induced by RNAi was demonstrated to result in irregular structure of PB in maize (Holding, 2014), wheat (Gil-Humanes et al, 2011), and rice (Kawakatsu et al, 2010;Nagamine et al, 2011), partial degradation has not ever been reported. Considering our results together with the fact that globulin accumulates on the surface of PB-II (Krishnan et al, 1992;Kumamaru et al, 2010) and its absence results in structurally deformed PB-II (Ashida et al, 2011), globulin protects glutelins from proteinase digestion and thereby facilitates stable glutelin accumulation.…”

Section: Compensation and Degradation In Glutelin And Globulin Mutantsmentioning

confidence: 97%

Glutelin is partially degraded in globulin-less mutants of rice (Oryza sativaL.)

Katsube-Tanaka

Khan

Yamaguchi

et al. 2016

Plant Production Science

View full text Add to dashboard Cite

a Graduate School of agriculture, Kyoto university, Kyoto, Japan;b Faculty of agriculture, tottori university, tottori, Japan; c national agricultural research center for Western region, Hiroshima, Japan ABSTRACT Multigenic glutelins and monogenic globulin are major storage proteins accumulating in vacuolederived protein body (PB-II) of rice (Oryza sativa L.) seeds. Because their interplay in PB-II formation was scarcely known, the effect of globulin-less mutation on glutelin accumulation was investigated. In globulin-less mutants, no phenotypic defect was found in seed and plant growth, while PB-II was deformed and apparent glutelin composition was changed, producing new glutelin α polypeptides X1-X5. 2D-PAGE of different combinations of globulin-less and glutelin subunit mutations suggested that the X1/X2, X3, and X4/X5 were derived from glutelin GluB1/GluB2/GluB4, GluA3, and GluA1/GluA2 subunits, respectively. Western blot with glutelin GluB4 subunit-specific and its variable region discriminable antibodies indicated at least in part the new spots X1/X2 are partially degraded products of GluB4 α polypeptides by the removal of 2-39 residues from C-terminus. Time course experiments with maturing seeds indicated the partial degradation of GluB4 occurred earlier (from 7 days after flowering) and higher than that of GluA1/GluA2. Considering the above results together with the fact that globulin accumulates at the periphery of PB-II and its absence produces deformed PB-II, globulin protects glutelins from proteinase digestion and thereby facilitates stable glutelin accumulation.

show abstract

Section: Compensation and Degradation In Glutelin And Globulin Mutantsmentioning

confidence: 97%

Glutelin is partially degraded in globulin-less mutants of rice (Oryza sativaL.)

Katsube-Tanaka

Khan

Yamaguchi

et al. 2016

Plant Production Science

View full text Add to dashboard Cite

show abstract

“…However, plants differ from animals in that they also produce different types of ER-derived vesicles, and these are involved in the accumulation of proteins (Galili, 2004;Hara-Nishimura et al, 2004;Herman and Schmidt, 2004;Herman, 2008). Protein bodies (PBs) store seed storage proteins in the endosperm of maize (Zea mays) and rice (Oryza sativa; Herman and Larkins, 1999;Satoh-Cruz et al, 2010;Nagamine et al, 2011). Precursoraccumulating vesicles accumulate seed protein precursors in the maturing cotyledons of pumpkin (Cucurbita maxima; Hara-Nishimura et al, 1998).…”

mentioning

confidence: 99%

Identification of Two Novel Endoplasmic Reticulum Body-Specific Integral Membrane Proteins

et al. 2012

View full text Add to dashboard Cite

The endoplasmic reticulum (ER) body, a large compartment specific to the Brassicales, accumulates b-glucosidase and possibly plays a role in the defense against pathogens and herbivores. Although the ER body is a subdomain of the ER, it is unclear whether any ER body-specific membrane protein exists. In this study, we identified two integral membrane proteins of the ER body in Arabidopsis (Arabidopsis thaliana) and termed them MEMBRANE PROTEIN OF ENDOPLASMIC RETICULUM BODY1 (MEB1) and MEB2. In Arabidopsis, a basic helix-loop-helix transcription factor, NAI1, and an ER body component, NAI2, regulate ER body formation. The expression profiles of MEB1 and MEB2 are similar to those of NAI1, NAI2, and ER body b-glucosidase PYK10 in Arabidopsis. The expression of MEB1 and MEB2 was reduced in the nai1 mutant, indicating that NAI1 regulates the expression of MEB1 and MEB2 genes. MEB1 and MEB2 proteins localize to the ER body membrane but not to the ER network, suggesting that these proteins are specifically recruited to the ER body membrane. MEB1 and MEB2 physically interacted with ER body component NAI2, and they were diffused throughout the ER network in the nai2 mutant, which has no ER body. Heterologous expression of MEB1 and MEB2 in yeast (Saccharomyces cerevisiae) suppresses iron and manganese toxicity, suggesting that MEB1 and MEB2 are metal transporters. These results indicate that the membrane of ER bodies has specific membrane proteins and suggest that the ER body is involved in defense against metal stress as well as pathogens and herbivores.

show abstract

“…The hydropathy plots of 13a prolamin suggest that the M and C domains are more hydrophobic than the N domain. 24) Therefore, 13a prolamin could aggregate in the ER via the hydrophobicity of the M and/or C domain.…”

Section: Discussionmentioning

confidence: 99%

Identification of the region of rice 13 kDa prolamin essential for the formation of ER-derived protein bodies using a heterologous expression system

Masumura

Shigemitsu

Morita

et al. 2015

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Cereal prolamins, which are alcohol-soluble seed storage proteins, can induce ER-derived protein bodies (PBs) in heterologous tissue. Like maize and wheat prolamins, rice prolamins can form ERderived PBs, but the region of mature polypeptides that is essential for PB formation has not been identified. In this study, we examined the formation mechanisms of ER-derived PB-like structures by expressing rice 13 kDa prolamin-deletion mutants fused to green fluorescent protein (GFP) in heterologous tissues such as yeast. The 13 kDa prolamin-GFP fusion protein was stably accumulated in transgenic yeast and formed an ER-derived PB-like structure. In contrast, rice α-globulin-GFP fusion protein was transported to vacuoles. In addition, the middle and COOH-terminal regions of 13 kDa prolamin formed ER-derived PB-like structures, whereas the NH 2 -terminal region of 13 kDa prolamin did not form such structures. These results suggest that the middle and COOH-terminal regions of 13 kDa prolamin can be retained and thus can induce ER-derived PB in yeast.

show abstract

A Role for the Cysteine-Rich 10 kDa Prolamin in Protein Body I Formation in Rice

Cited by 61 publications

References 40 publications

Glutelin is partially degraded in globulin-less mutants of rice (Oryza sativaL.)

Glutelin is partially degraded in globulin-less mutants of rice (Oryza sativaL.)

Identification of Two Novel Endoplasmic Reticulum Body-Specific Integral Membrane Proteins

Identification of the region of rice 13 kDa prolamin essential for the formation of ER-derived protein bodies using a heterologous expression system

Contact Info

Product

Resources

About