AustralieFrV1, Ncbi, Checkpoint, bibRecord, 000003

Genetic and Biochemical Evidence for the Involvement of α-1,4 Glucanotransferases in Amylopectin Synthesis1

Identifieur interne : 000003 ( Ncbi/Checkpoint ); précédent : 000002; suivant : 000004

Genetic and Biochemical Evidence for the Involvement of α-1,4 Glucanotransferases in Amylopectin Synthesis1

Auteurs : Christophe Colleoni ; David Dauvillée ; Gregory Mouille ; Alain Buléon ; Daniel Gallant ; Brigitte Bouchet ; Matthew Morell ; Michael Samuel ; Brigitte Delrue ; Christophe D'Hulst ; Christophe Bliard ; Jean-Marc Nuzillard ; Steven Ball

Source :

Plant Physiology [ 0032-0889 ] ; 1999.

RBID : PMC:59358

Abstract

We describe a novel mutation in the Chlamydomonas reinhardtii STA11 gene, which results in significantly reduced granular starch deposition and major modifications in amylopectin structure and granule shape. This defect simultaneously leads to the accumulation of linear malto-oligosaccharides. The sta11-1 mutation causes the absence of an α-1,4 glucanotransferase known as disproportionating enzyme (D-enzyme). D-enzyme activity was found to be correlated with the amount of wild-type allele doses in gene dosage experiments. All other enzymes involved in starch biosynthesis, including ADP-glucose pyrophosphorylase, debranching enzymes, soluble and granule-bound starch synthases, branching enzymes, phosphorylases, α-glucosidases (maltases), and amylases, were unaffected by the mutation. These data indicate that the D-enzyme is required for normal starch granule biogenesis in the monocellular alga C. reinhardtii.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC59358

PubMed: 10444082
PubMed Central: 59358

Affiliations:

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PMC:59358

Le document en format XML

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Genetic and Biochemical Evidence for the Involvement of α-1,4 Glucanotransferases in Amylopectin Synthesis<xref ref-type="fn" rid="FN1">1</xref>
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<author><name sortKey="Delrue, Brigitte" sort="Delrue, Brigitte" uniqKey="Delrue B" first="Brigitte" last="Delrue">Brigitte Delrue</name>
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<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="D Hulst, Christophe" sort="D Hulst, Christophe" uniqKey="D Hulst C" first="Christophe" last="D'Hulst">Christophe D'Hulst</name>
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<wicri:noCountry code="subfield">J.-M.N.)</wicri:noCountry>
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<author><name sortKey="Nuzillard, Jean Marc" sort="Nuzillard, Jean Marc" uniqKey="Nuzillard J" first="Jean-Marc" last="Nuzillard">Jean-Marc Nuzillard</name>
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<wicri:noCountry code="subfield">J.-M.N.)</wicri:noCountry>
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<front><div type="abstract" xml:lang="en"><p>We describe a novel mutation in the <italic>Chlamydomonas reinhardtii STA11</italic>
 gene, which results in significantly reduced granular starch deposition and major modifications in amylopectin structure and granule shape. This defect simultaneously leads to the accumulation of linear malto-oligosaccharides. The <italic>sta11</italic>
-<italic>1</italic>
 mutation causes the absence of an α-1,4 glucanotransferase known as disproportionating enzyme (D-enzyme). D-enzyme activity was found to be correlated with the amount of wild-type allele doses in gene dosage experiments. All other enzymes involved in starch biosynthesis, including ADP-glucose pyrophosphorylase, debranching enzymes, soluble and granule-bound starch synthases, branching enzymes, phosphorylases, α-glucosidases (maltases), and amylases, were unaffected by the mutation. These data indicate that the D-enzyme is required for normal starch granule biogenesis in the monocellular alga <italic>C. reinhardtii</italic>
.</p>
</div>
</front>
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<affiliations><list></list>
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<name sortKey="Bouchet, Brigitte" sort="Bouchet, Brigitte" uniqKey="Bouchet B" first="Brigitte" last="Bouchet">Brigitte Bouchet</name>
<name sortKey="Buleon, Alain" sort="Buleon, Alain" uniqKey="Buleon A" first="Alain" last="Buléon">Alain Buléon</name>
<name sortKey="Colleoni, Christophe" sort="Colleoni, Christophe" uniqKey="Colleoni C" first="Christophe" last="Colleoni">Christophe Colleoni</name>
<name sortKey="D Hulst, Christophe" sort="D Hulst, Christophe" uniqKey="D Hulst C" first="Christophe" last="D'Hulst">Christophe D'Hulst</name>
<name sortKey="Dauvillee, David" sort="Dauvillee, David" uniqKey="Dauvillee D" first="David" last="Dauvillée">David Dauvillée</name>
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<name sortKey="Gallant, Daniel" sort="Gallant, Daniel" uniqKey="Gallant D" first="Daniel" last="Gallant">Daniel Gallant</name>
<name sortKey="Morell, Matthew" sort="Morell, Matthew" uniqKey="Morell M" first="Matthew" last="Morell">Matthew Morell</name>
<name sortKey="Mouille, Gregory" sort="Mouille, Gregory" uniqKey="Mouille G" first="Gregory" last="Mouille">Gregory Mouille</name>
<name sortKey="Nuzillard, Jean Marc" sort="Nuzillard, Jean Marc" uniqKey="Nuzillard J" first="Jean-Marc" last="Nuzillard">Jean-Marc Nuzillard</name>
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Genetic and Biochemical Evidence for the Involvement of α-1,4 Glucanotransferases in Amylopectin Synthesis1

Genetic and Biochemical Evidence for the Involvement of α-1,4 Glucanotransferases in Amylopectin Synthesis1

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