Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia

This study reported the isolation and in silico characterization of full-length cellulose synthase (CesA) cDNA from Shorea parvifo/ia spp. parvifolia, an important tropical hardwood tree species- Cellulose synthase (CesA) is a member of processive glycosyltransferases that involved in cellulose bi...

Full description

Saved in:
Bibliographic Details
Main Authors: Lau, Ee Tiing, Ho, Wei Seng, Azlina, Binti Ahmadi Julaihi
Format: Article
Language:English
Published: Asian Network for Scientific Information 2009
Subjects:
Online Access:http://ir.unimas.my/id/eprint/29430/1/Molecular.pdf
http://ir.unimas.my/id/eprint/29430/
https://scialert.net/abstract/?doi=biotech.2009.416.424
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Universiti Malaysia Sarawak
Language: English
id my.unimas.ir.29430
record_format eprints
spelling my.unimas.ir.294302022-01-20T02:24:02Z http://ir.unimas.my/id/eprint/29430/ Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia Lau, Ee Tiing Ho, Wei Seng Azlina, Binti Ahmadi Julaihi QH Natural history QR Microbiology This study reported the isolation and in silico characterization of full-length cellulose synthase (CesA) cDNA from Shorea parvifo/ia spp. parvifolia, an important tropical hardwood tree species- Cellulose synthase (CesA) is a member of processive glycosyltransferases that involved in cellulose biosynthesis of plants, The full-length of SpCesAl cDNA with size 3308 and 3120 bp open reading frames encoding a 1040 amino acid was isolated using RT-PCR and RACE-PCR approaches, The predicted SpCesA} protein contained N-terminal cysteine rich zinc binding domain, 7 putative transmembrane helices (TMH), 4 U-motifs that contain a signature D, D, D; QxxRi•V motif, an alternating conserved region (CR-P) and 2 hypervariåble regions These entire shared domain structures suggest the functional role of SpCesAl is involved in cellulose biosynthesis in secondary vascular tissues of S. parvifolio spp. parvifolia. Sequence comparison also revealed the high similarity (87%) among SpCes,41 and PtrCesA2 of Populus tremuloidesw This further implies the involvement of SpCesA/ in catalyzes the cellulose biosynthesis of secondary cell wall rather than primary cell wall. Thus, identification of new CesA genes from tropical tree genomes is essential for enhancing knowledge Of cellulose biosynthesis in trees that has many fundamental and commercial implications. Asian Network for Scientific Information 2009 Article PeerReviewed text en http://ir.unimas.my/id/eprint/29430/1/Molecular.pdf Lau, Ee Tiing and Ho, Wei Seng and Azlina, Binti Ahmadi Julaihi (2009) Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia. Biotechnology, 8 (4). pp. 416-424. ISSN 1682-296X https://scialert.net/abstract/?doi=biotech.2009.416.424 DOI: 10.3923/biotech.2009.416.424
institution Universiti Malaysia Sarawak
building Centre for Academic Information Services (CAIS)
collection Institutional Repository
continent Asia
country Malaysia
content_provider Universiti Malaysia Sarawak
content_source UNIMAS Institutional Repository
url_provider http://ir.unimas.my/
language English
topic QH Natural history
QR Microbiology
spellingShingle QH Natural history
QR Microbiology
Lau, Ee Tiing
Ho, Wei Seng
Azlina, Binti Ahmadi Julaihi
Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
description This study reported the isolation and in silico characterization of full-length cellulose synthase (CesA) cDNA from Shorea parvifo/ia spp. parvifolia, an important tropical hardwood tree species- Cellulose synthase (CesA) is a member of processive glycosyltransferases that involved in cellulose biosynthesis of plants, The full-length of SpCesAl cDNA with size 3308 and 3120 bp open reading frames encoding a 1040 amino acid was isolated using RT-PCR and RACE-PCR approaches, The predicted SpCesA} protein contained N-terminal cysteine rich zinc binding domain, 7 putative transmembrane helices (TMH), 4 U-motifs that contain a signature D, D, D; QxxRi•V motif, an alternating conserved region (CR-P) and 2 hypervariåble regions These entire shared domain structures suggest the functional role of SpCesAl is involved in cellulose biosynthesis in secondary vascular tissues of S. parvifolio spp. parvifolia. Sequence comparison also revealed the high similarity (87%) among SpCes,41 and PtrCesA2 of Populus tremuloidesw This further implies the involvement of SpCesA/ in catalyzes the cellulose biosynthesis of secondary cell wall rather than primary cell wall. Thus, identification of new CesA genes from tropical tree genomes is essential for enhancing knowledge Of cellulose biosynthesis in trees that has many fundamental and commercial implications.
format Article
author Lau, Ee Tiing
Ho, Wei Seng
Azlina, Binti Ahmadi Julaihi
author_facet Lau, Ee Tiing
Ho, Wei Seng
Azlina, Binti Ahmadi Julaihi
author_sort Lau, Ee Tiing
title Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
title_short Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
title_full Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
title_fullStr Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
title_full_unstemmed Molecular Cloning of Cellulose Synthase Gene, SpCesA1 from Developing Xylem of Shorea parvifolia spp.parvifolia
title_sort molecular cloning of cellulose synthase gene, spcesa1 from developing xylem of shorea parvifolia spp.parvifolia
publisher Asian Network for Scientific Information
publishDate 2009
url http://ir.unimas.my/id/eprint/29430/1/Molecular.pdf
http://ir.unimas.my/id/eprint/29430/
https://scialert.net/abstract/?doi=biotech.2009.416.424
_version_ 1724078519197106176