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Accumulation of starch in Zn-deficient rice.

ABSTRACT: Zinc (Zn) is an essential micronutrient for living organisms, and understanding the molecular mechanisms of Zn deficiency may help to develop strategies to mitigate this problem. Microarray analysis of Zn deficient rice revealed the up-regulation of several genes involved in Zn transport. Moreover many genes involved in starch synthesis/transport were up-regulated by Zn deficiency in rice roots and shoots. Furthermore, starch granules were detected mainly in the cortical cells of these tissues. The gene encoding inactive RNase was much more highly transcribed than those encoding active RNases. Although the level of RNA degradation in a crude extract of Zn-deficient shoots was higher than that of Zn-sufficient shoots, addition of Zn significantly reduced the level of degradation. These results indicate that RNA degradation could be regulated by the amount of Zn in the cell, and that the tolerance of rice plants to low levels of Zn is promoted by the accumulation of starch and inactive RNase.

SUBMITTER: Suzuki M

PROVIDER: S-EPMC5520845 | biostudies-literature | 2012 Dec

REPOSITORIES: biostudies-literature

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Accumulation of starch in Zn-deficient rice.

Suzuki Motofumi M Bashir Khurram K Inoue Haruhiko H Takahashi Michiko M Nakanishi Hiromi H Nishizawa Naoko K NK

Rice (New York, N.Y.) 20120406 1

Zinc (Zn) is an essential micronutrient for living organisms, and understanding the molecular mechanisms of Zn deficiency may help to develop strategies to mitigate this problem. Microarray analysis of Zn deficient rice revealed the up-regulation of several genes involved in Zn transport. Moreover many genes involved in starch synthesis/transport were up-regulated by Zn deficiency in rice roots and shoots. Furthermore, starch granules were detected mainly in the cortical cells of these tissues. ...[more]

PMID: 27234235

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Project description:The gelatinization temperature of endosperm starch in most japonica rice cultivars is significantly lower than that in most indica rice cultivars. This is because three single nucleotide polymorphisms in the Starch synthase (SS) IIa gene in japonica rice cultivars (SSIIaJ ) significantly reduce SSIIa activity, resulting in an increase in amylopectin short chains with degree of polymerization (DP) ? 12 compared to indica rice cultivars (SSIIaI ). SSIIa forms a trimeric complex with SSI and starch branching enzyme (BE) IIb in maize and japonica rice, which is likely important for the biosynthesis of short and intermediate amylopectin chains (DP ? 24) within the amylopectin cluster. It was unknown whether the complete absence of SSIIa further increases amylopectin short chains and reduces gelatinization temperature and/or forms altered protein complexes due to the lack of a suitable mutant. Here, we identify the SSIIa-deficient mutant rice line EM204 (ss2a) from a screen of ca. 1,500 plants of the rice cultivar Kinmaze (japonica) that were subjected to N-methyl-N-nitrosourea mutagenesis. The SSIIa gene in EM204 was mutated at the boundary between intron 5 and exon 6, which generated a guanine to adenine mutation and resulted in deletion of exon 6 in the mRNA transcript. SSIIa activity and SSIIa protein in developing endosperm of EM204 were not detected by native-PAGE/SS activity staining and native-PAGE/immunoblotting, respectively. SSIIa protein was completely absent in mature seeds. Gel filtration chromatography of soluble protein extracted from developing seeds showed that the SSI elution pattern in EM204 was altered and more SSI was eluted around 300 kDa, which corresponds with the molecular weight of trimeric complexes in wild type. The apparent amylose content of EM204 rice grains was higher than that in its parent Kinmaze. EM204 also had higher content of amylopectin short chains (DP ? 12) than Kinmaze, which reduced the gelatinization temperature of EM204 starch by 5.6°C compared to Kinmaze. These results indicate that EM204 starch will be suitable for making foods and food additives that easily gelatinize and slowly retrograde.

Project description:Starch is the major component of cereal grains and is composed of essentially linear amylose and highly branched amylopectin. The properties and composition of starch determine the use and value of grains and their products. Starch synthase (SS) I, SSIIa, and SSIIIa play central roles in amylopectin biosynthesis. These three SS isozymes also affect seed development, as complete loss of both SSI and SSIIIa under reduced SSIIa activity in rice lead to sterility, whereas presence of minimal SSI or SSIIIa activity is sufficient for generating fertile seeds. SSs, branching enzymes, and/or debranching enzymes form protein complexes in cereal. However, the relationship between starch properties and the formation of protein complexes remain largely unknown. To better understand this phenomenon, properties of starch and protein complex formation were analyzed using developing mutant rice seeds (ss1 L /ss2a L /ss3a) in which all three major SS activities were reduced.The SS activity of ss1 L /ss2a L /ss3a was 25%-30% that of the wild-type. However, the grain weight of ss1 L /ss2a L /ss3a was 89% of the wild-type, 55% of which was starch, showing considerable starch synthesis. The reduction of soluble SS activity in ss1 L /ss2a L /ss3a resulted in increased levels of ADP-glucose pyrophosphorylase and granule-bound starch synthase I, which are responsible for substrate synthesis and amylose synthesis, respectively. Together, these features led to an increase in apparent amylose content (34%) in ss1 L /ss2a L /ss3a compared with wild-type (20%). Gel filtration chromatography of the soluble proteins in ss1 L /ss2a L /ss3a showed that the majority of the starch biosynthetic enzymes maintained the similar elution patterns as wild-type, except that the amounts of high-molecular-weight SSI (>?300 kDa) were reduced and SSIIa of approximately 200-300 kDa were present instead of those >?440 kDa, which predominate in wild-type. Immuno-precipitation analyses suggested that the interaction between the starch biosynthetic enzymes maybe reduced or weaker than in wild-type.Although major SS isozymes were simultaneously reduced in ss1 L /ss2a L /ss3a rice, active protein complexes were formed with a slightly altered pattern, suggesting that the assembly of protein complexes may be complemented among the SS isozymes. In addition, ss1 L /ss2a L /ss3a maintained the ability to synthesize starch and accumulated less amylopectin and more amylose in starch.

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Accumulation of starch in Zn-deficient rice.

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Accumulation of starch in Zn-deficient rice.

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