AustralieFrV1, Ncbi, Curation, bibRecord, 000004

Biochemical Characterization of the Chlamydomonas reinhardtii α-1,4 Glucanotransferase Supports a Direct Function in Amylopectin Biosynthesis1

Identifieur interne : 000004 ( Ncbi/Curation ); précédent : 000003; suivant : 000005

Biochemical Characterization of the Chlamydomonas reinhardtii α-1,4 Glucanotransferase Supports a Direct Function in Amylopectin Biosynthesis1

Auteurs : Christophe Colleoni ; David Dauvillée ; Gregory Mouille ; Matthew Morell ; Michael Samuel ; Marie-Christine Slomiany ; Luc Liénard ; Fabrice Wattebled ; Christophe D'Hulst ; Steven Ball

Source :

Plant Physiology [ 0032-0889 ] ; 1999.

RBID : PMC:59333

Abstract

Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of Chlamydomonas reinhardtii sta11-1 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in sta11-1 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the sta11-1 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC59333

PubMed: 10444083
PubMed Central: 59333

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PMC:59333

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Christophe Colleoni

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

David Dauvillée

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Gregory Mouille

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Matthew Morell

<affiliation><nlm:aff id="N0x8c805b0N0x98d96cc">Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600, Canberra, Australian Capital Territory 2601, Australia (M.M., M.S.)</nlm:aff>
<wicri:noCountry code="subfield">M.S.)</wicri:noCountry>
</affiliation>

Michael Samuel

<affiliation><nlm:aff id="N0x8c805b0N0x98d96cc">Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600, Canberra, Australian Capital Territory 2601, Australia (M.M., M.S.)</nlm:aff>
<wicri:noCountry code="subfield">M.S.)</wicri:noCountry>
</affiliation>

Marie-Christine Slomiany

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Luc Liénard

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Fabrice Wattebled

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Christophe D'Hulst

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

Steven Ball

<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>

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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Biochemical Characterization of the <italic>Chlamydomonas reinhardtii</italic>
 α-1,4 Glucanotransferase Supports a Direct Function in Amylopectin Biosynthesis<xref ref-type="fn" rid="FN1">1</xref>
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<author><name sortKey="Colleoni, Christophe" sort="Colleoni, Christophe" uniqKey="Colleoni C" first="Christophe" last="Colleoni">Christophe Colleoni</name>
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<author><name sortKey="Dauvillee, David" sort="Dauvillee, David" uniqKey="Dauvillee D" first="David" last="Dauvillée">David Dauvillée</name>
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<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
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<wicri:noCountry code="subfield">M.S.)</wicri:noCountry>
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<author><name sortKey="Samuel, Michael" sort="Samuel, Michael" uniqKey="Samuel M" first="Michael" last="Samuel">Michael Samuel</name>
<affiliation><nlm:aff id="N0x8c805b0N0x98d96cc">Commonwealth Scientific and Industrial Research Organization, Division of Plant Industry, G.P.O. Box 1600, Canberra, Australian Capital Territory 2601, Australia (M.M., M.S.)</nlm:aff>
<wicri:noCountry code="subfield">M.S.)</wicri:noCountry>
</affiliation>
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<author><name sortKey="Slomiany, Marie Christine" sort="Slomiany, Marie Christine" uniqKey="Slomiany M" first="Marie-Christine" last="Slomiany">Marie-Christine Slomiany</name>
<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
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<author><name sortKey="Lienard, Luc" sort="Lienard, Luc" uniqKey="Lienard L" first="Luc" last="Liénard">Luc Liénard</name>
<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
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<author><name sortKey="Wattebled, Fabrice" sort="Wattebled, Fabrice" uniqKey="Wattebled F" first="Fabrice" last="Wattebled">Fabrice Wattebled</name>
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<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">S.B.)</wicri:noCountry>
</affiliation>
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<author><name sortKey="Ball, Steven" sort="Ball, Steven" uniqKey="Ball S" first="Steven" last="Ball">Steven Ball</name>
<affiliation><nlm:aff id="N0x8c805b0N0x98d95d0">Laboratoire de Chimie Biologique, Unité Mixte de Recherche du Centre National de la Recherche Scientifique no. 8576, Université des Sciences et Technologies de Lille, 59655 Villeneuve d'Ascq cedex, France (C.C., D.D., G.M., M.-C.S., L.L., F.W., C.d.H., S.B.)</nlm:aff>
<wicri:noCountry code="subfield">S.B.)</wicri:noCountry>
</affiliation>
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<series><title level="j">Plant Physiology</title>
<idno type="ISSN">0032-0889</idno>
<idno type="eISSN">1532-2548</idno>
<imprint><date when="1999">1999</date>
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<front><div type="abstract" xml:lang="en"><p>Plant α-1,4 glucanotransferases (disproportionating enzymes, or D-enzymes) transfer glucan chains among oligosaccharides with the concomitant release of glucose (Glc). Analysis of <italic>Chlamydomonas reinhardtii sta11</italic>
-<italic>1</italic>
 mutants revealed a correlation between a D-enzyme deficiency and specific alterations in amylopectin structure and starch biosynthesis, thereby suggesting previously unknown biosynthetic functions. This study characterized the biochemical activities of the α-1,4 glucanotransferase that is deficient in <italic>sta11</italic>
-<italic>1</italic>
 mutants. The enzyme exhibited the glucan transfer and Glc production activities that define D-enzymes. D-enzyme also transferred glucans among the outer chains of amylopectin (using the polysaccharide chains as both donor and acceptor) and from malto-oligosaccharides into the outer chains of either amylopectin or glycogen. In contrast to transfer among oligosaccharides, which occurs readily with maltotriose, transfer into polysaccharide required longer donor molecules. All three enzymatic activities, evolution of Glc from oligosaccharides, glucan transfer from oligosaccharides into polysaccharides, and transfer among polysaccharide outer chains, were evident in a single 62-kD band. Absence of all three activities co-segregated with the <italic>sta11</italic>
-<italic>1</italic>
 mutation, which is known to cause abnormal accumulation of oligosaccharides at the expense of starch. To explain these data we propose that D-enzymes function directly in building the amylopectin structure.</p>
</div>
</front>
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Biochemical Characterization of the Chlamydomonas reinhardtii α-1,4 Glucanotransferase Supports a Direct Function in Amylopectin Biosynthesis1

Biochemical Characterization of the Chlamydomonas reinhardtii α-1,4 Glucanotransferase Supports a Direct Function in Amylopectin Biosynthesis1

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