Xylem-specific and tension stress-responsive expression of cellulose synthase genes from aspen trees.
Identifieur interne : 004363 ( Main/Exploration ); précédent : 004362; suivant : 004364Xylem-specific and tension stress-responsive expression of cellulose synthase genes from aspen trees.
Auteurs : Chandrashekhar P. Joshi [États-Unis]Source :
- Applied biochemistry and biotechnology [ 0273-2289 ] ; 2003.
Descripteurs français
- KwdFr :
- Arabidopsis (enzymologie), Arabidopsis (génétique), Cellulose (biosynthèse), Cellulose (génétique), Glucosyltransferases (génétique), Populus (enzymologie), Populus (génétique), Régulation de l'expression des gènes codant pour des enzymes (MeSH), Régulation de l'expression des gènes végétaux (MeSH), Sous-unités de protéines (composition chimique), Sous-unités de protéines (génétique), Structures de plante (enzymologie).
- MESH :
- biosynthèse : Cellulose.
- composition chimique : Sous-unités de protéines.
- enzymologie : Arabidopsis, Populus, Structures de plante.
- génétique : Arabidopsis, Cellulose, Glucosyltransferases, Populus, Sous-unités de protéines.
- Régulation de l'expression des gènes codant pour des enzymes, Régulation de l'expression des gènes végétaux.
English descriptors
- KwdEn :
- Arabidopsis (enzymology), Arabidopsis (genetics), Cellulose (biosynthesis), Cellulose (genetics), Gene Expression Regulation, Enzymologic (MeSH), Gene Expression Regulation, Plant (MeSH), Glucosyltransferases (genetics), Plant Structures (enzymology), Populus (enzymology), Populus (genetics), Protein Subunits (chemistry), Protein Subunits (genetics).
- MESH :
- chemical , biosynthesis : Cellulose.
- chemical , chemistry : Protein Subunits.
- enzymology : Arabidopsis, Plant Structures, Populus.
- genetics : Arabidopsis, Cellulose, Glucosyltransferases, Populus, Protein Subunits.
- Gene Expression Regulation, Enzymologic, Gene Expression Regulation, Plant.
Abstract
Genetic improvement of cellulose biosynthesis in woody trees is one of the major goals of tree biotechnology research. Yet, progress in this field has been slow owing to (1) unavailability of key genes from tree genomes, (2) the inability to isolate active and intact cellulose synthase complexes and, (3) the limited understanding of the mechanistic processes involved in the wood cellulose development. Here I report on the recent advances in molecular genetics of cellulose synthases (CesA) from aspen trees. Two different types of cellulose synthases appear to be involved in cellulose deposition in primary and secondary walls in aspen xylem. The three distinct secondary CesAs from aspen- PtrCesA1, PtrCesA2, and PtrCesA3-appear to be aspen homologs of Arabidopsis secondary CesAs AtCesA8, AtCesA7, and AtCesA4, respectively, based on their high identity/similarity (>80%). These aspen CesA proteins share the transmembrane domain (TMD) structure that is typical of all known "true" CesA proteins: two TMDs toward the N-terminal and six TMDs toward the C-terminal. The putative catalytic domain is present between TMDs 2 and 3. All signature motifs of processive glycosyltransferases are also present in this catalytic domain. In a phylogenetic tree based on various predicted CesA proteins from Arabidopsis and aspen, aspen CesAs fall into families similar to those seen with Arabidopsis CesAs, suggesting their functional similarity. The coordinate expression of three aspen secondary CesAs in xylem and phloem fibers, along with their simultaneous tension stress-responsive upregulation, suggests that these three CesAs may play a pivotal role in biosynthesis of better-quality cellulose in secondary cell walls of plants. These results are likely to have a direct impact on genetic manipulation of trees in the future.
DOI: 10.1385/abab:105:1-3:17
PubMed: 12721472
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Yet, progress in this field has been slow owing to (1) unavailability of key genes from tree genomes, (2) the inability to isolate active and intact cellulose synthase complexes and, (3) the limited understanding of the mechanistic processes involved in the wood cellulose development. Here I report on the recent advances in molecular genetics of cellulose synthases (CesA) from aspen trees. Two different types of cellulose synthases appear to be involved in cellulose deposition in primary and secondary walls in aspen xylem. The three distinct secondary CesAs from aspen- PtrCesA1, PtrCesA2, and PtrCesA3-appear to be aspen homologs of Arabidopsis secondary CesAs AtCesA8, AtCesA7, and AtCesA4, respectively, based on their high identity/similarity (>80%). These aspen CesA proteins share the transmembrane domain (TMD) structure that is typical of all known "true" CesA proteins: two TMDs toward the N-terminal and six TMDs toward the C-terminal. The putative catalytic domain is present between TMDs 2 and 3. All signature motifs of processive glycosyltransferases are also present in this catalytic domain. In a phylogenetic tree based on various predicted CesA proteins from Arabidopsis and aspen, aspen CesAs fall into families similar to those seen with Arabidopsis CesAs, suggesting their functional similarity. The coordinate expression of three aspen secondary CesAs in xylem and phloem fibers, along with their simultaneous tension stress-responsive upregulation, suggests that these three CesAs may play a pivotal role in biosynthesis of better-quality cellulose in secondary cell walls of plants. 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Yet, progress in this field has been slow owing to (1) unavailability of key genes from tree genomes, (2) the inability to isolate active and intact cellulose synthase complexes and, (3) the limited understanding of the mechanistic processes involved in the wood cellulose development. Here I report on the recent advances in molecular genetics of cellulose synthases (CesA) from aspen trees. Two different types of cellulose synthases appear to be involved in cellulose deposition in primary and secondary walls in aspen xylem. The three distinct secondary CesAs from aspen- PtrCesA1, PtrCesA2, and PtrCesA3-appear to be aspen homologs of Arabidopsis secondary CesAs AtCesA8, AtCesA7, and AtCesA4, respectively, based on their high identity/similarity (>80%). These aspen CesA proteins share the transmembrane domain (TMD) structure that is typical of all known "true" CesA proteins: two TMDs toward the N-terminal and six TMDs toward the C-terminal. The putative catalytic domain is present between TMDs 2 and 3. All signature motifs of processive glycosyltransferases are also present in this catalytic domain. In a phylogenetic tree based on various predicted CesA proteins from Arabidopsis and aspen, aspen CesAs fall into families similar to those seen with Arabidopsis CesAs, suggesting their functional similarity. The coordinate expression of three aspen secondary CesAs in xylem and phloem fibers, along with their simultaneous tension stress-responsive upregulation, suggests that these three CesAs may play a pivotal role in biosynthesis of better-quality cellulose in secondary cell walls of plants. 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