Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase.

Pear, Julie R.; Kawagoe, Yasuhiro; Schreckengost, William E.; Delmer, Deborah P.; Stalker, David M.

doi:10.1073/pnas.93.22.12637

Cited by 658 publications

(556 citation statements)

References 30 publications

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“…Besides, sequence analysis revealed existence of the motif D, D, D, QxxRW (motifs indicative of processive glycosyltransferase) (Saxena and Brown, 1995). It was shown that GhCESA1 was able to bind to the substrate UDP-glucose and the expression patterns of GhCesA1 and GhCesA2 were tightly linked with the timing of cellulose biosynthesis (Pear et al, 1996). Collectively, these findings supported the hypothesis that GhCesA1 and GhCesA2 encoded potential catalytic subunits of CelS which may be associated with biogenesis of microfibrils of cellulose .…”

Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gsupporting

confidence: 73%

“…The identification of potential components of the plant CelS complex was achieved by a molecular approach. Two cDNA clones GhCESA1 and GhCESA2 were identified in cotton fiber enriched in cellulose (Pear et al, 1996). These cDNAs encoded proteins with some similarity to the bacterial CESA proteins.…”

Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gmentioning

confidence: 99%

“…After six years, the first plant CesAs, GhCesA1 and GhCesA2 were identified in cotton (Pear et al, 1996).…”

Section: Structural Features Of Cesa Proteinsmentioning

confidence: 99%

“…The gene responsible for this phenotype was isolated by map-based cloning. Sequence analysis revealed that the amino acid Ala 549 in the wild-type was substituted by Val 549 in rsw1 and that this gene encoded the catalytic subunit of CESA based on homology with cotton CESAs (Pear et al, 1996). Reverse genetics experiments were used to show that the cloned wild-type AtCesA1 gene complements the rsw1 mutant.…”

Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gmentioning

confidence: 99%

“…(iv) Globular domain A and B: the globular domains A and B are highly conserved among CESAs (Pear et al, 1996;Wu et al, 2000;Joshi, 2003b;Joshi et al, 2004); (Joshi, 2003a,b;Joshi et al, 2004).…”

Section: Structural Features Of Cesa Proteinsmentioning

confidence: 99%

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Structure, organization, and functions of cellulose synthase complexes in higher plants

Festucci-Buselli

Otoni

Joshi

2007

Braz. J. Plant Physiol.

116

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Annually, plants produce about 180 billion tons of cellulose making it the largest reservoir of organic carbon on Earth. Cellulose is a linear homopolymer of beta(1-4)-linked glucose residues. The coordinated synthesis of glucose chains is orchestrated by specific plasma membrane-bound cellulose synthase complexes (CelS). The CelS is postulated to be composed of approximately 36 cellulose synthase (CESA) subunits. The CelS synthesizes 36 glucose chains in close proximity before they are further organized into microfibrils that are further associated with other cell wall polymers. The 36 glucose chains in a microfibril are stabilized by intra- and inter-hydrogen bonding which confer great stability on microfibrils. Several elementary microfibrils come together to form macrofibrils. Many CESA isoforms appear to be involved in the cellulose biosynthetic process and at least three types of CESA isoforms appear to be necessary for the functional organization of CelS in higher plants.

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Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gsupporting

confidence: 73%

Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gmentioning

confidence: 99%

“…After six years, the first plant CesAs, GhCesA1 and GhCesA2 were identified in cotton (Pear et al, 1996).…”

Section: Structural Features Of Cesa Proteinsmentioning

confidence: 99%

Section: Cels Is Composed Of Cesa Isoforms That Are Encoded By Cesa Gmentioning

confidence: 99%

Section: Structural Features Of Cesa Proteinsmentioning

confidence: 99%

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Structure, organization, and functions of cellulose synthase complexes in higher plants

Festucci-Buselli

Otoni

Joshi

2007

Braz. J. Plant Physiol.

116

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Epidermis

2006

Esau's Plant Anatomy

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Cellulose

French

Bertoniere

Brown

et al. 2003

Kirk-Othmer Encyclopedia of Chemical Technology

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This article covers nomenclature, sources, preparation, uses, microcrystalline cellulose, structural chemistry, reactions, solvents, and liquid crystals. Cellulose for commercial purposes comes mostly from wood and cotton, whereas cellulose for research comes from bacteria, algae, and ramie (also a textile fiber). Preparation includes pulping and purification, with an alternative method of steam explosion. The pore structure of cellulose is mentioned, along with the buildup of cellulose molecules into entire fibers. Emphasis is given to cellulose crystal structure. Recent research has provided structures with much better resolution for two crystal forms. Most native cellulose is a mixture of two crystalline phases. Cellulose solutions are important to the rayon and cellophane industries, and new solvents are of interest because they may lessen pollution and might permit commercial production of stronger cellulosic materials through the formation of liquid crystals. Figures include the chemical and physical structures of the molecule, including in solution, X‐ray diffraction patterns, the structure of a microfibril, and the unit cell structures of cellulose I–IV.

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Higher plants contain homologs of the bacterial celA genes encoding the catalytic subunit of cellulose synthase.

Abstract: In spite of much effort, no one has succeeded in isolating and characterizing the enzyme(s) responsible for synthesis of cellulose, the major cell wall polymer of plants. We have characterized two cotton (Gossypium hirsutum) cDNA clones and identified one rice (Oryza sativa) cDNA that are

Cited by 658 publications

References 30 publications

Structure, organization, and functions of cellulose synthase complexes in higher plants

Structure, organization, and functions of cellulose synthase complexes in higher plants

Epidermis

Cellulose

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