Molecular analysis of the waxy locus of Zea mays

Klösgen, Ralf Bernd; Gierl, Alfons; Schwarz‐Sommer, Zsuzsanna; Saedler, Heinz

doi:10.1007/bf00333960

Cited by 262 publications

(127 citation statements)

References 46 publications

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“…The accession numbers for the plants described in Figure 2B are as follows: barley (Hordeum vulgare), X07932 (Rohde et al, 1988); wheatI (Triticum aestivum), X57233 (Clark et al, 1991); maize (Zea mays), X03935 (Klosgen et al, 1986); sorghum (Sorghum bicolor), Q43134 (Y.C. Hsing, unpublished data); rice (Oryza sativa), X62134 (R.J. Okayaki, unpublished data); bean (Phaseolus vulgaris), AB029546 (N. Isono, K. Nozaki, H. Ito, H. Matsui, and M. Honma, un-…”

Section: Accession Numbersmentioning

confidence: 99%

Discrete Forms of Amylose Are Synthesized by Isoforms of GBSSI in Pea[W]

Edwards

Vincken²,

Suurs³

et al. 2002

The Plant Cell

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Amyloses with distinct molecular masses are found in the starch of pea embryos compared with the starch of pea leaves. In pea embryos, a granule-bound starch synthase protein (GBSSIa) is required for the synthesis of a significant portion of the amylose. However, this protein seems to be insignificant in the synthesis of amylose in pea leaves. cDNA clones encoding a second isoform of GBSSI, GBSSIb, have been isolated from pea leaves. Comparison of GBSSIa and GBSSIb activities shows them to have distinct properties. These differences have been confirmed by the expression of GBSSIa and GBSSIb in the amylose-free mutant of potato. GBSSIa and GBSSIb make distinct forms of amylose that differ in their molecular mass. These differences in product specificity, coupled with differences in the tissues in which GBSSIa and GBSSIb are most active, explain the distinct forms of amylose found in different tissues of pea. The shorter form of amylose formed by GBSSIa confers less susceptibility to the retrogradation of starch pastes than the amylose formed by GBSSIb. The product specificity of GBSSIa could provide beneficial attributes to starches for food and nonfood uses.

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Section: Accession Numbersmentioning

confidence: 99%

Discrete Forms of Amylose Are Synthesized by Isoforms of GBSSI in Pea[W]

Edwards

Vincken²,

Suurs³

et al. 2002

The Plant Cell

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“…The C-terminal 1,000-amino acid residues from wheat SSIII, potato SSIII, and maize SSIII (DU1) were used in the analysis as inclusion of the entire amino acid sequences for these genes and could not be analyzed by the PILEUP (a Genetics Computer Group program). The sequences used are: maize GBSS (Kloesgen et al, 1986), rice GBSS (Okagaki, 1992), wheat GBSS (Clark et al, 1991), potato GBSS (van der Leij et al, 1991), pea GBSS (Dry et al, 1992), maize SSI , rice SSI (Baba et al, 1993), wheat SSI (Li et al, 1999a), potato SSI (GenBank accession no. Y10416), wheat SSIIA (Li et al, 1999b), maize SSIIa and SSIIb ), pea SSII (Dry et al, 1992, potatoSSII (Edwards et al, 1995), maize SSIII (DU1; the product of the du1 gene; Gao et al, 1998), wheat SSIII (wSSIII.B3; this paper), potato SSIII (Abel et al, 1996), cowpea SSIII (GenBank accession no.…”

Section: N-terminal Variable Repeat Regionmentioning

confidence: 99%

“…So far, four classes of SSs have been found in higher plants: granule-bound SS (GBSS; Kloesgen et al, 1986;van der Leij et al, 1991;Okagaki, 1992), SSI (Baba et al, 1993;Knight et al, 1998), SSII (Dry et al, 1992;Edwards et al, 1995;Harn et al, 1998), and SSIII (Abel et al, 1996;Marshall et al, 1996;Gao et al, 1998). In cereals, the most comprehensively studied species is maize, where in addition to GBSS, cDNAs encoding SSI, SSIIa, and SSIIb have been isolated.…”

mentioning

confidence: 99%

The Structure and Expression of the Wheat Starch Synthase III Gene. Motifs in the Expressed Gene Define the Lineage of the Starch Synthase III Gene Family

Mouille²,

Kosar-Hashemi

et al. 2000

Plant Physiology

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The endosperm of hexaploid wheat (Triticum aestivum [L.]) was shown to contain a high molecular weight starch synthase (SS) analogous to the product of the maize du1 gene, starch synthase III (SSIII; DU1). cDNA and genomic DNA sequences encoding wheat SSIII were isolated and characterized. The wheat SSIII cDNA is 5,346 bp long and contains an open reading frame that encodes a 1,628-amino acid polypeptide. A putative N-terminal transit peptide, a 436-amino acid C-terminal catalytic domain, and a central 470-amino acid SSIII-specific domain containing three regions of repeated amino acid similarity were identified in the wheat gene. A fourth region between the transit peptide and the SSIII-specific domain contains repeat motifs that are variable with respect to motif sequence and repeat number between wheat and maize. In dicots, this N-terminal region does not contain repeat motifs and is truncated. The gene encoding wheat SSIII, designated ss3, consists of 16 exons extending over 10 kb, and is located on wheat chromosome I. Expression of ss3 mRNA in wheat was detected in leaves, pre-anthesis florets, and from very early to middle stage of endosperm development. The entire N-terminal variable repeat region and the majority of the SSIII-specific domain are encoded on a single 2,703-bp exon. A gene encoding a class III SS from the Arabidopsis genome sequencing project shows a strongly conserved exon structure to the wheat ss3 gene, with the exception of the N-terminal region. The evolutionary relationships of the genes encoding monocot and dicot class III SSs are discussed.

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“…All are highly similar in the C-terminal region, a span of approximately 450 amino acid residues comprising the catalytic and starch-binding domains, but differ significantly in the sequences of their N termini, with SSIII having the longest N-terminal arm. Genetic analyses in plants that accumulate storage starch indicate that at least three of the SS classes provide unique functions in starch biosynthesis: GBSS (Shure et al, 1983;Klö sgen et al, 1986); SSIII (Gao et al, 1998;Cao et al, 1999); and SSII (Craig et al, 1998;Morell et al, 2003;Zhang et al, 2004). Mutations in these SS genes cause specific alterations in starch composition and/or starch structure, demonstrating that the function of each of these isoforms is not fully compensated by any other SS.…”

mentioning

confidence: 99%

Mutations Affecting Starch Synthase III in Arabidopsis Alter Leaf Starch Structure and Increase the Rate of Starch Synthesis

2005

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The role of starch synthase (SS) III (SSIII) in the synthesis of transient starch in Arabidopsis (Arabidopsis thaliana) was investigated by characterizing the effects of two insertion mutations at the AtSS3 gene locus. Both mutations, termed Atss3-1 and Atss3-2, condition complete loss of SSIII activity and prevent normal gene expression at both the mRNA and protein levels. The mutations cause a starch excess phenotype in leaves during the light period of the growth cycle due to an apparent increase in the rate of starch synthesis. In addition, both mutations alter the physical structure of leaf starch. Significant increases were noted in the mutants in the frequency of linear chains in amylopectin with a degree of polymerization greater than approximately 60, and relatively small changes were observed in chains of degree of polymerization 4 to 50. Furthermore, starch in the Atss3-1 and Atss3-2 mutants has a higher phosphate content, approximately two times that of wild-type leaf starch. Total SS activity is increased in both Atss3 mutants and a specific SS activity appears to be up-regulated. The data indicate that, in addition to its expected direct role in starch assembly, SSIII also has a negative regulatory function in the biosynthesis of transient starch in Arabidopsis.Starch serves a fundamental role in the life cycle of plants as the primary carbohydrate storage form for chemical energy. Transient starch is produced and degraded over short periods of time to satisfy the ongoing energy requirements of plant development (e.g. over the course of the diurnal cycle in the leaf). In contrast, storage starch accumulates and persists in heterotrophic tissues in anticipation of future plant energy needs, such as germination or sprouting. The anabolism and catabolism of both storage and transient starch forms requires precise control of the expression and/or activity of many different enzymes.Starch consists of two homopolymers of a-D-glucosyl units joined in linear arrays by a-(1!4) glycosidic bonds, amylose (Am) and amylopectin (Ap). Ap is the more abundant polymer, and it contains a-(1!6) branch linkages at a frequency of approximately 5%. The organized architectural arrangement of linear and branched chains in Ap enables efficient packaging of large amounts of Glc into insoluble starch granules. The basic enzymatic steps responsible for Ap structure begin with the formation of the activated glucosyl donor ADP-Glc (ADPG), catalyzed by ADPG pyrophosphorylase. Reactions utilizing ADPG to build a-(1!4)-linked linear glucosyl chains are catalyzed by the starch synthases (SSs). Branch linkages are introduced by branching enzymes (BEs), which catalyze cleavage of an internal a-(1!4) linkage and creation of a new a-(1!6) linkage by transfer of the released reducing end to a C6 hydroxyl. Starch-debranching enzymes (DBEs) hydrolyze branch linkages and are thought to be involved in starch biosynthesis, based on evidence that DBE mutants produce less starch than normal and contain a highly branched polysaccharide not obse...

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Molecular analysis of the waxy locus of Zea mays

Cited by 262 publications

References 46 publications

Discrete Forms of Amylose Are Synthesized by Isoforms of GBSSI in Pea[W]

Discrete Forms of Amylose Are Synthesized by Isoforms of GBSSI in Pea[W]

The Structure and Expression of the Wheat Starch Synthase III Gene. Motifs in the Expressed Gene Define the Lineage of the Starch Synthase III Gene Family

Mutations Affecting Starch Synthase III in Arabidopsis Alter Leaf Starch Structure and Increase the Rate of Starch Synthesis

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