Identification of four starch‐branching enzymes in barley endosperm: partial purification of forms I, IIa and IIb

Sun, Chuanxin; Sathish, P.; Ahlandsberg, Staffan; Deiber, Anna; Jansson, Christer

doi:10.1046/j.1469-8137.1997.00796.x

Cited by 39 publications

(23 citation statements)

References 19 publications

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“…af064563), although the corresponding region of the gene is covered. It is interesting that in barley (in contrast to maize) the relative activities of SBEIIa and SBEIIb in the endosperm (as measure by phosphorylation stimulation) appear to be comparable with each other (Sun et al, 1997). Thus the situation in barley appears to be in between the two extremes of wheat (SBEIIa predominant in soluble phase) and maize (SBEIIb predominant in soluble phase).…”

Section: Discussionmentioning

confidence: 92%

“…In rice (Oryza sativa), two isoforms of SBE II, IIa and IIb, are found in the endosperm, but IIb is the major isoform and unique to the endosperm (Yamanouchi and Nakamura, 1992). In barley (Hordeum vulgare), both SBEIIa and SBEIIb forms show comparable activities in the endosperm (Sun et al, 1997) but the IIb form is only expressed in the endosperm. In contrast to these examples, anionexchange chromatography of wheat soluble extracts yielded a single peak of SBEII activity , and a single N-terminal sequence was obtained .…”

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confidence: 99%

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Comparison of Starch-Branching Enzyme Genes Reveals Evolutionary Relationships Among Isoforms. Characterization of a Gene for Starch-Branching Enzyme IIa from the Wheat D Genome DonorAegilops tauschii

et al. 2001

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Genes and cDNAs for starch-branching enzyme II (SBEII) have been isolated from libraries constructed from Aegilops tauschii and wheat (Triticum aestivum) endosperm, respectively. One class of genes has been termed wSBEII-DA1 and encodes the N terminus reported for an SBEII from wheat endosperm. On the basis of phylogenetic comparisons with other branching enzyme sequences, wSBEII-DA1 is considered to be a member of the SBEIIa class. The wSBEII-DA1 gene consists of 22 exons with exons 4 to 21 being identical in length to the maize (Zea mays) SBEIIb gene, and the gene is located in the proximal region of the long arm of chromosome 2 at a locus designated sbe2a. RNA encoding SBEIIa can be detected in the endosperm from 6 d after flowering and is at its maximum level from 15 to 18 d after anthesis. Use of antibodies specific for SBEIIa demonstrated that this protein was present in both the soluble and granule bound fractions in developing wheat endosperm. We also report a cDNA sequence for SBEIIa that could arise by variant transcription/splicing. A second gene, termed wSBEII-DB1, was isolated and encodes an SBEII, which shows greater sequence identity with SBEIIb-type sequences than with SBEIIa-type sequences. Comparisons of SBEII gene structures among wheat, maize, and Arabidopsis indicate the lineage of the SBEII genes.

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Section: Discussionmentioning

confidence: 92%

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confidence: 99%

Comparison of Starch-Branching Enzyme Genes Reveals Evolutionary Relationships Among Isoforms. Characterization of a Gene for Starch-Branching Enzyme IIa from the Wheat D Genome DonorAegilops tauschii

et al. 2001

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“…Antisera were produced by AgriSera (Vännäs, Sweden) after immunizing rabbits with the Coomassie Brilliant Blue R 250-stained SUSIBA2-70 and SUSIBA2-68 polypeptide bands excised from the SDS gel. Protein gel blot analysis was performed as described (Sun et al, 1997). Polyclonal His tag antibodies were purchased from Santa Cruz Biotechnology (Santa Cruz, CA).…”

Section: Overproduction Of Susiba2 In Escherichia Coli Microsequencimentioning

confidence: 99%

“…Overexpression was performed according to the manual provided by the manufacturer, except that the isopropylthio-␤-galactoside induction was performed at 37ЊC for 2 h. The overproduced protein was purified by fast protein liquid chromatography on a column with a Ni ϩ chelating resin. SDS-PAGE was run as described previously (Sun et al, 1997).…”

Section: Overproduction Of Susiba2 In Escherichia Coli Microsequencimentioning

confidence: 99%

A Novel WRKY Transcription Factor, SUSIBA2, Participates in Sugar Signaling in Barley by Binding to the Sugar-Responsive Elements of theiso1Promoter [W]

et al. 2003

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SURE (sugar responsive) is a cis element in plant sugar signaling. The SURE element was reported first for potato, in which it confers sugar responsiveness to the patatin promoter. A SURE binding transcription factor has not been isolated. We have isolated a transcription factor cDNA from barley and purified the corresponding protein. The transcription factor, SUSIBA2 (sugar signaling in barley), belongs to the WRKY proteins and was shown to bind to SURE and W-box elements but not to the SP8a element in the iso1 promoter. Nuclear localization of SUSIBA2 was demonstrated in a transient assay system with a SUSIBA2:green fluorescent protein fusion protein. Exploiting the novel transcription factor oligodeoxynucleotide decoy strategy with transformed barley endosperm provided experimental evidence for the importance of the SURE elements in iso1 transcription. Antibodies against SUSIBA2 were produced, and the expression pattern for susiba2 was determined at the RNA and protein levels. It was found that susiba2 is expressed in endosperm but not in leaves. Transcription of susiba2 is sugar inducible, and ectopic susiba2 expression was obtained in sugar-treated leaves. Likewise, binding to SURE elements was observed for nuclear extracts from sugar-treated but not from control barley leaves. The temporal expression of susiba2 in barley endosperm followed that of iso1 and endogenous sucrose levels, with a peak at ‫ف‬ 12 days after pollination. Our data indicate that SUSIBA2 binds to the SURE elements in the barley iso1 promoter as an activator. Furthermore, they show that SUSIBA2 is a regulatory transcription factor in starch synthesis and demonstrate the involvement of a WRKY protein in carbohydrate anabolism. Orthologs to SUSIBA2 were isolated from rice and wheat endosperm.

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“…BE is the only enzyme that can introduce ␣-1,6-glucosidic linkages into ␣-polyglucans and, therefore, it plays an essential role in the biosynthesis of amylopectin. The BEs from various higher plants appear to be composed of two types, namely BEI and BEII from maize (Zea mays; Boyer and Preiss, 1978a;Fisher and Boyer, 1983;Guan and Preiss, 1993;Guan et al, 1997), wheat (Triticum aestivum; Morell et al, 1997), and barley (Hordeum vulgare; Sun et al, 1997), and the A-type and B-type from pea (Pisum sativum; Burton et al, 1995;Martin and Smith, 1995) and potato (Solanum tuberosum; Larsson et al, 1996Larsson et al, , 1998. At least three isoforms of BE have been identified in rice (Oryza sativa) endosperm (Mizuno et al, 1992;Nakamura et al, 1992).…”

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Biochemical and Genetic Analysis of the Effects ofAmylose-Extender Mutation in Rice Endosperm

et al. 2001

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Biochemical analysis of amylose-extender (ae) mutant of rice (Oryza sativa) revealed that the mutation in the gene for starch-branching enzyme IIb (BEIIb) specifically altered the structure of amylopectin in the endosperm by reducing short chains with degree of polymerization of 17 or less, with the greatest decrease in chains with degree of polymerization of 8 to 12. The extent of such change was correlated with the gelatinization properties of the starch granules, as determined in terms of solubility in urea solution. The ae mutation caused a dramatic reduction in the activity of BEIIb. The activity of soluble starch synthase I (SSI) in the ae mutant was significantly lower than in the wild type, suggesting that the mutation had a pleiotropic effect on the SSI activity. In contrast, the activities of BEI, BEIIa, ADP-Glc pyrophosphorylase, isoamylase, isoamylase, pullulanase, and Suc synthase were not affected by the mutation. Therefore, it is stressed that the function of BEIIb cannot be complemented by BEIIa and BEI. These results strongly suggest that BEIIb plays a specific role in the transfer of short chains, which might then be extended by SS to form the A and B 1 chains of amylopectin cluster in rice endosperm.Starch is composed of two types of molecule, namely amylose and amylopectin. Amylose is an essentially linear molecule composed of ␣(134)-linked glucosidic chains, whereas amylopectin is a highly branched glucan with ␣(136) glucosidic bonds that connect linear chains. The ␣-1,4 chains of amylopectin consist of A chains that carry no additional chains, B chains that carry A chains or other B chains, and a C chain that includes the reducing terminus (Peat et al., 1952). Hizukuri (1986) proposed a cluster model for amylopectin. In this model, A and B 1 chains form a single cluster, whereas B 2 and B 3 chains extend to two and three clusters, respectively. Hanashiro et al. (1996) proposed that, in amylopectin, chains of degree of polymerization (DP) Ϲ12, 13 Ϲ DP Ϲ 24, 25 Ϲ DP Ϲ 36, and DP м 37 correspond to A chains, B 1 chains, B 2 chains, and B 3 and longer chains, respectively.

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Identification of four starch‐branching enzymes in barley endosperm: partial purification of forms I, IIa and IIb

Cited by 39 publications

References 19 publications

Comparison of Starch-Branching Enzyme Genes Reveals Evolutionary Relationships Among Isoforms. Characterization of a Gene for Starch-Branching Enzyme IIa from the Wheat D Genome DonorAegilops tauschii

Comparison of Starch-Branching Enzyme Genes Reveals Evolutionary Relationships Among Isoforms. Characterization of a Gene for Starch-Branching Enzyme IIa from the Wheat D Genome DonorAegilops tauschii

A Novel WRKY Transcription Factor, SUSIBA2, Participates in Sugar Signaling in Barley by Binding to the Sugar-Responsive Elements of theiso1Promoter [W]

Biochemical and Genetic Analysis of the Effects ofAmylose-Extender Mutation in Rice Endosperm

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