NDLI: Xylem-specific and tension stress-responsive expression of cellulose synthase genes from aspen trees

Content Provider	Springer Nature Link
Author	Joshi, Chandrashekhar P.
Copyright Year	2003
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.
Starting Page	17
Ending Page	25
Page Count	9
File Format	PDF
ISSN	02732289
Journal	Applied Biochemistry and Biotechnology
Volume Number	105
Issue Number	1-3
e-ISSN	15590291
Language	English
Publisher	Humana Press
Publisher Date	2003-01-01
Publisher Place	Totowa
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biotechnology Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Environmental Engineering Biochemistry Bioengineering Applied Microbiology and Biotechnology Biotechnology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Xylem-specific and tension stress-responsive coexpression of KORRIGAN endoglucanase and three secondary wall-associated cellulose synthase genes in aspen trees

Differential expression patterns of two cellulose synthase genes are associated with primary and secondary cell wall development in aspen trees

A xylem-specific cellulose synthase gene from aspen (Populus tremuloides) is responsive to mechanical stress.

Production of bacterial cellulose from alternate feedstocks

Molecular Characterization and Expression Analyses of an Anthocyanin Synthase Gene from Magnolia sprengeri Pamp.

Heterologous Expression of Two Ferulic Acid Esterases from Penicillium funiculosum

Erratum to: Expression Profiling of Bioactive Genes from a Medicinal Plant Nigella sativa L.

Heterologous Expression, Purification, and Biochemical Characterization of α-Humulene Synthase from Zingiber zerumbet Smith

Cellulose production based on hemicellulose hydrolysate from steam-pretreated willow

Xylem-specific and tension stress-responsive expression of cellulose synthase genes from aspen trees

Similar Documents

Xylem-specific and tension stress-responsive coexpression of KORRIGAN endoglucanase and three secondary wall-associated cellulose synthase genes in aspen trees

Differential expression patterns of two cellulose synthase genes are associated with primary and secondary cell wall development in aspen trees

A xylem-specific cellulose synthase gene from aspen (Populus tremuloides) is responsive to mechanical stress.

Production of bacterial cellulose from alternate feedstocks

Molecular Characterization and Expression Analyses of an Anthocyanin Synthase Gene from Magnolia sprengeri Pamp.

Heterologous Expression of Two Ferulic Acid Esterases from Penicillium funiculosum

Erratum to: Expression Profiling of Bioactive Genes from a Medicinal Plant Nigella sativa L.

Heterologous Expression, Purification, and Biochemical Characterization of α-Humulene Synthase from Zingiber zerumbet Smith

Cellulose production based on hemicellulose hydrolysate from steam-pretreated willow

Xylem-specific and tension stress-responsive expression of cellulose synthase genes from aspen trees