Expression, organisation and structure of the genes encoding the waxy protein (granule-bound starch synthase) in wheat

Ainsworth, Claire; Clark, Joanna; Balsdon, J.T.

doi:10.1007/bf00038996

Cited by 101 publications

(53 citation statements)

References 40 publications

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“…Inukai et al (2000) characterized the M8F (74-8) mutant, which is one of the four wx leaky mutants screened by Amano (1985), at the molecular level and one amino acid substitution (IIe-182 to Asn-182 change) was also found in exon 5. This residue is conserved between the five plant species except for pea (Ainsworth et al 1993). We reported that the expression level of the Wx protein in Milky Queen was almost the same as that in Koshihikari (Sato et al 2001).…”

Section: Discussionmentioning

confidence: 91%

“…1). Both amino acid residues were conserved among the six waxy protein sequences derived from wheat, barley, maize, potato, pea and rice (Ainsworth et al 1993). Inukai et al (2000) characterized the M8F (74-8) mutant, which is one of the four wx leaky mutants screened by Amano (1985), at the molecular level and one amino acid substitution (IIe-182 to Asn-182 change) was also found in exon 5.…”

Section: Discussionmentioning

confidence: 99%

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Molecular Characterization of Wx-mq, a Novel Mutant Gene for Low-amylose Content in Endosperm of Rice (Oryza sativa L.).

et al. 2002

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In this paper, we characterized the Wx-mq gene for low amylose content in a rice variety, Milky Queen, at the molecular level. The Wx-mq gene was cloned by RT-PCR, and a nearly full-length cDNA sequence of the gene was determined. Sequence comparison between the Wx-mq gene and the wild type allele (Wx-b), cloned from cv. Koshihikari, revealed that two base changes existed within the coding region; a G to A base change at nucleotide position 497 and a T to C base change at nucleotide position 595. Each nucleotide substitution should generate a missense base change (an Arg-158 to His-158 change in exon4, and a Tyr-191 to His-191 change in exon5). However, it is not known which missense mutation is essential for the activity of the WX protein. To identify rice varieties and lines, which harbored the Wx-mq gene, PCR primers were designed at the gene level. These primers were able to amplify the Wx-mq specific 741 bp band in Milky Queen, and in other rice variety and lines, Milky Princess, Joiku 436 and Etsunan 190, all of which have the same pedigree as that of Milky Queen. On the other hand, no 741 bp band was amplified with the primers in Koshihikari which harbored the wild type allele (Wx-b), and the other low-amylose content variety and line, Snow Pearl and NM391, which do not have the pedigree. Thus, it is possible to detect the Wx-mq gene by PCR.

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Section: Discussionmentioning

confidence: 91%

Section: Discussionmentioning

confidence: 99%

Molecular Characterization of Wx-mq, a Novel Mutant Gene for Low-amylose Content in Endosperm of Rice (Oryza sativa L.).

et al. 2002

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“…The dendrogram was generated using the PileUp program from Genetics Computer Group (Devereaux et al, 1984). The amino acid sequences used for the analysis are as follows (accession numbers given where reference not cited): wheat GBSS (Ainsworth et al, 1993), wheat SSI , wheat SSII-A, wheat SSII-B, and wheat SSII-D (this paper), rice GBSS (X62134), rice SSI (D16202), maize GBSS (M24258), maize SSI (AF036891), maize SSIIa and maize SSIIb (Harn et al, 1998), maize SSII (Gao et al, 1998), pea GBSS (X88789), pea SSII (X88790), potato GBSS (X58453), potato SSI (Y10416), potato SSII (X87988), potato SSIII (X94400), and E. coli glycogen synthase (GS; J01616). Five groups of enzymes are labeled as GBSS, SSI, SSII, SSIII, and GS.…”

Section: The Sequences Of the Sgp-1 Proteins Are Highly Homologous Tomentioning

confidence: 99%

“…Conserved regions are shown in bold and transit peptides (where defined) are shown in gray. Amino acid sequences were deduced from genes encoding; wheat GBSS (Ainsworth et al, 1993), wheat SSI , wheat SSII-A1 (this report), maize SSIIa cDNA (Harn et al, 1998), and the maize dull-1 gene (Gao et al, 1998). The sequences of the conserved regions are defined in Figure 2. class II SSs range from 49% identity with potato SSII to 70% identity with maize SSIIa.…”

Section: The Sequences Of the Sgp-1 Proteins Are Highly Homologous Tomentioning

confidence: 99%

The Localization and Expression of the Class II Starch Synthases of Wheat1

Chu

Mouille

et al. 1999

Plant Physiology

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The starch granules of hexaploid wheat (Triticum aestivum) contain a group of three proteins known as SGP-1 (starch granule protein-1) proteins, which have apparent molecular masses of 100, 108, and 115 kD. The nature and role of these proteins has not been defined previously. We demonstrate that these polypeptides are starch synthases that are present in both the starch granule and the soluble fraction at the early stages of wheat endosperm development, but that are exclusively granule bound at mid and late endosperm development. A partial cDNA clone encoding a fragment of the 100-kD protein was obtained by screening a wheat endosperm cDNA expression library using monoclonal antibodies. Three classes of cDNA were subsequently isolated from a wheat endosperm cDNA library by nucleic acid hybridization and were shown to encode the 100-, 108-, and 115-kD proteins. The cDNA sequences are highly homologous to class II starch synthases and have the highest homology with the maize SSIIa (starch synthase IIa) gene. mRNA for the SGP-1 proteins was detected in the leaf, pre-anthesis florets, and endosperm of wheat and is highly expressed in the leaf and in the grain during the early to mid stages of development. We discuss the roles of the SGP-1 proteins in starch biosynthesis in wheat.

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“…DNA and RNA gel blot hybridization analyses were performed as described by Ainsworth et al (1993). Twenty micrograms of total RNA was used per lane.…”

Section: Gel Blot Analysismentioning

confidence: 99%

Male and female flowers of the dioecious plant sorrel show different patterns of MADS box gene expression.

et al. 1995

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Male and female flowers of the dioecious plant sorrel (Rumex acetosa) each produce three whorls of developed floral organs: two similar whorls of three perianth segments and either six stamens (in the male) or a gynoecium consisting of a fertile carpel and two sterile carpels (in the female). In the developing male flower, there is no significant proliferation of cells in the center of the flower, in the position normally occupied by the carpels of a hermaphrodite plant. In the female flower, small stamen primordia are formed. To determine whether the organ differences are associated with differences in the expression of organ identity genes, cDNA clones representing the putative homologs of B and C function MADS box genes were isolated and used in an in situ hybridization analysis. The expression of R A D l and RADP (two different DEFlClENS homologs) in males and females was confined to the stamen whorl; the lack of expression in the second, inner perianth whorl correlated with the sepaloid nature of the inner whorl of perianth segments. Expression of R A P l (a PLENA homolog) occurred in the carpel and stamen whorls in very young flower primordia from both males and females. However, as soon as the inappropriate set of organs ceased to develop, R A P l expression became undetectable in those organs. The absence of expression of R A P l may be the cause of the arrest in organ development or may be a consequence.

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Expression, organisation and structure of the genes encoding the waxy protein (granule-bound starch synthase) in wheat

Cited by 101 publications

References 40 publications

Molecular Characterization of Wx-mq, a Novel Mutant Gene for Low-amylose Content in Endosperm of Rice (Oryza sativa L.).

Molecular Characterization of Wx-mq, a Novel Mutant Gene for Low-amylose Content in Endosperm of Rice (Oryza sativa L.).

The Localization and Expression of the Class II Starch Synthases of Wheat1

Male and female flowers of the dioecious plant sorrel show different patterns of MADS box gene expression.

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