PoplarV1, Main, Exploration, bibRecord, 001A22

A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.

Identifieur interne : 001A22 ( Main/Exploration ); précédent : 001A21; suivant : 001A23

A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.

Auteurs : Pallinti Purushotham [États-Unis] ; Sung Hyun Cho [États-Unis] ; Sara M. Díaz-Moreno [Suède] ; Manish Kumar [États-Unis] ; B Tracy Nixon [États-Unis] ; Vincent Bulone [Australie] ; Jochen Zimmer [États-Unis]

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2016.

RBID : pubmed:27647898

Descripteurs français

KwdFr :
- Alignement de séquences (MeSH), Biocatalyse (MeSH), Cellulase (métabolisme), Cellulose (biosynthèse), Cellulose (ultrastructure), Cinétique (MeSH), Cytosol (métabolisme), Domaines protéiques (MeSH), Facteurs temps (MeSH), Glucosyltransferases (composition chimique), Glucosyltransferases (isolement et purification), Glucosyltransferases (métabolisme), Hydrolyse (MeSH), Hétérosides (métabolisme), Isoenzymes (composition chimique), Isoenzymes (métabolisme), Lipides (composition chimique), Microfibrilles (métabolisme), Microfibrilles (ultrastructure), Populus (enzymologie), Protéines recombinantes (composition chimique), Protéines recombinantes (isolement et purification), Protéines végétales (composition chimique), Protéines végétales (isolement et purification), Protéines végétales (métabolisme), Spectrométrie de masse (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- biosynthèse : Cellulose.
- composition chimique : Glucosyltransferases, Isoenzymes, Lipides, Protéines recombinantes, Protéines végétales.
- enzymologie : Populus.
- isolement et purification : Glucosyltransferases, Protéines recombinantes, Protéines végétales.
- métabolisme : Cellulase, Cytosol, Glucosyltransferases, Hétérosides, Isoenzymes, Microfibrilles, Protéines végétales.
- ultrastructure : Alignement de séquences, Biocatalyse, Cellulose, Cinétique, Domaines protéiques, Facteurs temps, Hydrolyse, Microfibrilles, Spectrométrie de masse, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Biocatalysis (MeSH), Cellulase (metabolism), Cellulose (biosynthesis), Cellulose (ultrastructure), Cytosol (metabolism), Glucosyltransferases (chemistry), Glucosyltransferases (isolation & purification), Glucosyltransferases (metabolism), Glycosides (metabolism), Hydrolysis (MeSH), Isoenzymes (chemistry), Isoenzymes (metabolism), Kinetics (MeSH), Lipids (chemistry), Mass Spectrometry (MeSH), Microfibrils (metabolism), Microfibrils (ultrastructure), Plant Proteins (chemistry), Plant Proteins (isolation & purification), Plant Proteins (metabolism), Populus (enzymology), Protein Domains (MeSH), Recombinant Proteins (chemistry), Recombinant Proteins (isolation & purification), Sequence Alignment (MeSH), Time Factors (MeSH).
MESH :
- chemical , biosynthesis : Cellulose.
- chemical , chemistry : Glucosyltransferases, Isoenzymes, Lipids, Plant Proteins, Recombinant Proteins.
- chemical , isolation & purification : Glucosyltransferases, Plant Proteins, Recombinant Proteins.
- chemical , metabolism : Cellulase, Glucosyltransferases, Glycosides, Isoenzymes, Plant Proteins.
- chemical , ultrastructure : Cellulose.
- enzymology : Populus.
- metabolism : Cytosol, Microfibrils.
- ultrastructure : Microfibrils.
- Amino Acid Sequence, Biocatalysis, Hydrolysis, Kinetics, Mass Spectrometry, Protein Domains, Sequence Alignment, Time Factors.

Abstract

Plant cell walls are a composite material of polysaccharides, proteins, and other noncarbohydrate polymers. In the majority of plant tissues, the most abundant polysaccharide is cellulose, a linear polymer of glucose molecules. As the load-bearing component of the cell wall, individual cellulose chains are frequently bundled into micro and macrofibrils and are wrapped around the cell. Cellulose is synthesized by membrane-integrated and processive glycosyltransferases that polymerize UDP-activated glucose and secrete the nascent polymer through a channel formed by their own transmembrane regions. Plants express several different cellulose synthase isoforms during primary and secondary cell wall formation; however, so far, none has been functionally reconstituted in vitro for detailed biochemical analyses. Here we report the heterologous expression, purification, and functional reconstitution of Populus tremula x tremuloides CesA8 (PttCesA8), implicated in secondary cell wall formation. The recombinant enzyme polymerizes UDP-activated glucose to cellulose, as determined by enzyme degradation, permethylation glycosyl linkage analysis, electron microscopy, and mutagenesis studies. Catalytic activity is dependent on the presence of a lipid bilayer environment and divalent manganese cations. Further, electron microscopy analyses reveal that PttCesA8 produces cellulose fibers several micrometers long that occasionally are capped by globular particles, likely representing PttCesA8 complexes. Deletion of the enzyme's N-terminal RING-finger domain almost completely abolishes fiber formation but not cellulose biosynthetic activity. Our results demonstrate that reconstituted PttCesA8 is not only sufficient for cellulose biosynthesis in vitro but also suffices to bundle individual glucan chains into cellulose microfibrils.

DOI: 10.1073/pnas.1606210113
PubMed: 27647898
PubMed Central: PMC5056052

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Biocatalysis (MeSH)</term>
<term>Cellulase (metabolism)</term>
<term>Cellulose (biosynthesis)</term>
<term>Cellulose (ultrastructure)</term>
<term>Cytosol (metabolism)</term>
<term>Glucosyltransferases (chemistry)</term>
<term>Glucosyltransferases (isolation & purification)</term>
<term>Glucosyltransferases (metabolism)</term>
<term>Glycosides (metabolism)</term>
<term>Hydrolysis (MeSH)</term>
<term>Isoenzymes (chemistry)</term>
<term>Isoenzymes (metabolism)</term>
<term>Kinetics (MeSH)</term>
<term>Lipids (chemistry)</term>
<term>Mass Spectrometry (MeSH)</term>
<term>Microfibrils (metabolism)</term>
<term>Microfibrils (ultrastructure)</term>
<term>Plant Proteins (chemistry)</term>
<term>Plant Proteins (isolation & purification)</term>
<term>Plant Proteins (metabolism)</term>
<term>Populus (enzymology)</term>
<term>Protein Domains (MeSH)</term>
<term>Recombinant Proteins (chemistry)</term>
<term>Recombinant Proteins (isolation & purification)</term>
<term>Sequence Alignment (MeSH)</term>
<term>Time Factors (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Alignement de séquences (MeSH)</term>
<term>Biocatalyse (MeSH)</term>
<term>Cellulase (métabolisme)</term>
<term>Cellulose (biosynthèse)</term>
<term>Cellulose (ultrastructure)</term>
<term>Cinétique (MeSH)</term>
<term>Cytosol (métabolisme)</term>
<term>Domaines protéiques (MeSH)</term>
<term>Facteurs temps (MeSH)</term>
<term>Glucosyltransferases (composition chimique)</term>
<term>Glucosyltransferases (isolement et purification)</term>
<term>Glucosyltransferases (métabolisme)</term>
<term>Hydrolyse (MeSH)</term>
<term>Hétérosides (métabolisme)</term>
<term>Isoenzymes (composition chimique)</term>
<term>Isoenzymes (métabolisme)</term>
<term>Lipides (composition chimique)</term>
<term>Microfibrilles (métabolisme)</term>
<term>Microfibrilles (ultrastructure)</term>
<term>Populus (enzymologie)</term>
<term>Protéines recombinantes (composition chimique)</term>
<term>Protéines recombinantes (isolement et purification)</term>
<term>Protéines végétales (composition chimique)</term>
<term>Protéines végétales (isolement et purification)</term>
<term>Protéines végétales (métabolisme)</term>
<term>Spectrométrie de masse (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Cellulose</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glucosyltransferases</term>
<term>Isoenzymes</term>
<term>Lipids</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Glucosyltransferases</term>
<term>Plant Proteins</term>
<term>Recombinant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cellulase</term>
<term>Glucosyltransferases</term>
<term>Glycosides</term>
<term>Isoenzymes</term>
<term>Plant Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="ultrastructure" xml:lang="en"><term>Cellulose</term>
</keywords>
<keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Cellulose</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glucosyltransferases</term>
<term>Isoenzymes</term>
<term>Lipides</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Populus</term>
</keywords>
<keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Glucosyltransferases</term>
<term>Protéines recombinantes</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cytosol</term>
<term>Microfibrils</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cellulase</term>
<term>Cytosol</term>
<term>Glucosyltransferases</term>
<term>Hétérosides</term>
<term>Isoenzymes</term>
<term>Microfibrilles</term>
<term>Protéines végétales</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Microfibrils</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Biocatalysis</term>
<term>Hydrolysis</term>
<term>Kinetics</term>
<term>Mass Spectrometry</term>
<term>Protein Domains</term>
<term>Sequence Alignment</term>
<term>Time Factors</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="fr"><term>Alignement de séquences</term>
<term>Biocatalyse</term>
<term>Cellulose</term>
<term>Cinétique</term>
<term>Domaines protéiques</term>
<term>Facteurs temps</term>
<term>Hydrolyse</term>
<term>Microfibrilles</term>
<term>Spectrométrie de masse</term>
<term>Séquence d'acides aminés</term>
</keywords>
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<front><div type="abstract" xml:lang="en">Plant cell walls are a composite material of polysaccharides, proteins, and other noncarbohydrate polymers. In the majority of plant tissues, the most abundant polysaccharide is cellulose, a linear polymer of glucose molecules. As the load-bearing component of the cell wall, individual cellulose chains are frequently bundled into micro and macrofibrils and are wrapped around the cell. Cellulose is synthesized by membrane-integrated and processive glycosyltransferases that polymerize UDP-activated glucose and secrete the nascent polymer through a channel formed by their own transmembrane regions. Plants express several different cellulose synthase isoforms during primary and secondary cell wall formation; however, so far, none has been functionally reconstituted in vitro for detailed biochemical analyses. Here we report the heterologous expression, purification, and functional reconstitution of Populus tremula x tremuloides CesA8 (PttCesA8), implicated in secondary cell wall formation. The recombinant enzyme polymerizes UDP-activated glucose to cellulose, as determined by enzyme degradation, permethylation glycosyl linkage analysis, electron microscopy, and mutagenesis studies. Catalytic activity is dependent on the presence of a lipid bilayer environment and divalent manganese cations. Further, electron microscopy analyses reveal that PttCesA8 produces cellulose fibers several micrometers long that occasionally are capped by globular particles, likely representing PttCesA8 complexes. Deletion of the enzyme's N-terminal RING-finger domain almost completely abolishes fiber formation but not cellulose biosynthetic activity. Our results demonstrate that reconstituted PttCesA8 is not only sufficient for cellulose biosynthesis in vitro but also suffices to bundle individual glucan chains into cellulose microfibrils.</div>
</front>
</TEI>
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<DateCompleted><Year>2018</Year>
<Month>01</Month>
<Day>26</Day>
</DateCompleted>
<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<Month>10</Month>
<Day>04</Day>
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<Title>Proceedings of the National Academy of Sciences of the United States of America</Title>
<ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation>
</Journal>
<ArticleTitle>A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.</ArticleTitle>
<Pagination><MedlinePgn>11360-11365</MedlinePgn>
</Pagination>
<Abstract><AbstractText>Plant cell walls are a composite material of polysaccharides, proteins, and other noncarbohydrate polymers. In the majority of plant tissues, the most abundant polysaccharide is cellulose, a linear polymer of glucose molecules. As the load-bearing component of the cell wall, individual cellulose chains are frequently bundled into micro and macrofibrils and are wrapped around the cell. Cellulose is synthesized by membrane-integrated and processive glycosyltransferases that polymerize UDP-activated glucose and secrete the nascent polymer through a channel formed by their own transmembrane regions. Plants express several different cellulose synthase isoforms during primary and secondary cell wall formation; however, so far, none has been functionally reconstituted in vitro for detailed biochemical analyses. Here we report the heterologous expression, purification, and functional reconstitution of Populus tremula x tremuloides CesA8 (PttCesA8), implicated in secondary cell wall formation. The recombinant enzyme polymerizes UDP-activated glucose to cellulose, as determined by enzyme degradation, permethylation glycosyl linkage analysis, electron microscopy, and mutagenesis studies. Catalytic activity is dependent on the presence of a lipid bilayer environment and divalent manganese cations. Further, electron microscopy analyses reveal that PttCesA8 produces cellulose fibers several micrometers long that occasionally are capped by globular particles, likely representing PttCesA8 complexes. Deletion of the enzyme's N-terminal RING-finger domain almost completely abolishes fiber formation but not cellulose biosynthetic activity. Our results demonstrate that reconstituted PttCesA8 is not only sufficient for cellulose biosynthesis in vitro but also suffices to bundle individual glucan chains into cellulose microfibrils.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Purushotham</LastName>
<ForeName>Pallinti</ForeName>
<Initials>P</Initials>
<AffiliationInfo><Affiliation>Department of Molecular Physiology and Biological Physics, University of Virginia School of Medicine, Charlottesville, VA 22908.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cho</LastName>
<ForeName>Sung Hyun</ForeName>
<Initials>SH</Initials>
<AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Díaz-Moreno</LastName>
<ForeName>Sara M</ForeName>
<Initials>SM</Initials>
<AffiliationInfo><Affiliation>Division of Glycoscience, Royal Institute of Technology, Stockholm, SE-10691, Sweden.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Kumar</LastName>
<ForeName>Manish</ForeName>
<Initials>M</Initials>
<AffiliationInfo><Affiliation>Department of Chemical Engineering, The Pennsylvania State University, University Park, PA 16802.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Nixon</LastName>
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A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.

A single heterologously expressed plant cellulose synthase isoform is sufficient for cellulose microfibril formation in vitro.

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