Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains

Kurek, Isaac; Kawagoe, Yasuhiro; Jacob-Wilk, Deborah; Doblin, Monika S.; Delmer, Deborah P.

doi:10.1073/pnas.162077099

Cited by 227 publications

(177 citation statements)

References 36 publications

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“…Our results demonstrated that AtCESA2 could homodimerize and that the zinc finger domain of AtCESA2 was important for the interaction (Fig. 8B), consistent with previously reported results (Kurek et al, 2002). In contrast, no E3 ligase activity was detected in the in vitro assay for detecting the E3 ligase activity of RING finger proteins (data not shown).…”

Section: Atcesa2 Interacts With Itself Through the N-terminal Zinc-bisupporting

confidence: 93%

“…8A). Kurek et al (2002) confirmed that GhCESA1 could form homodimers as well as heterodimers with GhCESA2 through the zinc-binding domain. To investigate whether AtCESA2 can homodimerize and to identify the domain responsible, we performed a yeast (Saccharomyces cerevisiae) two-hybrid assay with different truncations of AtCESA2 protein.…”

Section: Atcesa2 Interacts With Itself Through the N-terminal Zinc-bimentioning

confidence: 58%

“…Kurek et al (2002) reported that cotton fiber cellulose synthase catalytic subunits dimerized via the N-terminal zinc finger domains. Our yeast two-hybrid experiment suggested that AtCESA2 could homodimerize via the zinc finger domains.…”

Section: Components and Formation Of Cesa Rosettesmentioning

confidence: 99%

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Knockout of the AtCESA2 Gene Affects Microtubule Orientation and Causes Abnormal Cell Expansion in Arabidopsis

Chu¹,

Chen²,

Zhang³

et al. 2006

Plant Physiol.

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Complete cellulose synthesis is required to form functional cell walls and to facilitate proper cell expansion during plant growth. AtCESA2 is a member of the cellulose synthase A family in Arabidopsis (Arabidopsis thaliana) that participates in cell wall formation. By analysis of transgenic seedlings, we demonstrated that AtCESA2 was expressed in all organs, except root hairs. The atcesa2 mutant was devoid of AtCESA2 expression, leading to the stunted growth of hypocotyls in seedlings and greatly reduced seed production in mature plants. These observations were attributed to alterations in cell size as a result of reduced cellulose synthesis in the mutant. The orientation of microtubules was also altered in the atcesa2 mutant, which was clearly observed in hypocotyls and petioles. Complementary expression of AtCESA2 in atcesa2 could rescue the mutant phenotypes. Together, we conclude that disruption of cellulose synthesis results in altered orientation of microtubules and eventually leads to abnormal plant growth. We also demonstrated that the zinc finger-like domain of AtCESA2 could homodimerize, possibly contributing to rosette assemblies of cellulose synthase A within plasma membranes.

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Section: Atcesa2 Interacts With Itself Through the N-terminal Zinc-bisupporting

confidence: 93%

Section: Atcesa2 Interacts With Itself Through the N-terminal Zinc-bimentioning

confidence: 58%

See 1 more Smart Citation

Knockout of the AtCESA2 Gene Affects Microtubule Orientation and Causes Abnormal Cell Expansion in Arabidopsis

Chu¹,

Chen²,

Zhang³

et al. 2006

Plant Physiol.

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“…Tests of protein-protein interactions in the yeast (Saccharomyces cerevisiae) two-hybrid system did not reveal any interactions between the second cytoplasmic domains of CesA proteins, and the second cytoplasmic domains did not show any interactions with the first cytoplasmic domains (data not shown). The first cytoplasmic domains of CesA proteins have been shown recently to interact with each other and are proposed to mediate the formation of the rosette complexes (Kurek et al, 2002). Our data suggest that the second cytoplamsic domains of AtCesA proteins might not be involved in direct interactions between CesA polypeptides; rather, they might mediate interactions of CesA proteins with other cellular components in the rosette complex.…”

Section: Possible Mechanisms For the Dominant Negative Effect Of The mentioning

confidence: 65%

Expression of a Mutant Form of Cellulose Synthase AtCesA7 Causes Dominant Negative Effect on Cellulose Biosynthesis

Zhong

Morrison²,

Freshour³

et al. 2003

Plant Physiology

132

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Cellulose synthase catalytic subunits (CesAs) have been implicated in catalyzing the biosynthesis of cellulose, the major component of plant cell walls. Interactions between CesA subunits are thought to be required for normal cellulose synthesis, which suggests that incorporation of defective CesA subunits into cellulose synthase complex could potentially cause a dominant effect on cellulose synthesis. However, all CesA mutants so far reported have been shown to be recessive in terms of cellulose synthesis. In the course of studying the molecular mechanisms regulating secondary wall formation in fibers, we have found that a mutant allele of AtCesA7 gene in the fra5 (fragile fiber 5) mutant causes a semidominant phenotype in the reduction of fiber cell wall thickness and cellulose content. The fra5 missense mutation occurred in a conserved amino acid located in the second cytoplasmic domain of AtCesA7. Overexpression of the fra5 mutant cDNA in wild-type plants not only reduced secondary wall thickness and cellulose content but also decreased primary wall thickness and cell elongation. In contrast, overexpression of the fra6 mutant form of AtCesA8 did not cause any reduction in cell wall thickness and cellulose content. These results suggest that the fra5 mutant protein may interfere with the function of endogenous wild-type CesA proteins, thus resulting in a dominant negative effect on cellulose biosynthesis.Cellulose is the most abundant biopolymer produced by plants. It is the major component of plant cell walls and, in particular, is synthesized in large quantities during secondary wall formation of tracheary elements and fibers in wood. Cellulose synthase, the enzyme responsible for cellulose biosynthesis, is located in the plasma membrane. It is imaged by transmission electron microscopy as a rosette consisting of six particles, which is termed the terminal rosette complex (Brown and Montezinos, 1976). The identification of the rosette complexes as the sites of cellulose synthesis was confirmed by the immunolocation of putative cellulose synthase catalytic subunits (CesAs) in the rosette subunits (Kimura et al., 1999). It is proposed that as many as 36 CesA protein molecules together with other putative associated proteins form one rosette complex, which produces 36 (1,4)-␤-glucan chains that polymerize and crystallize into a microfibril with an estimated diameter of 8 to10 nm (Ha et al., 1998). The monosaccharide donor substrate used by CesAs, UDP-Glc, has been postulated to be provided by membrane-associated form(s) of Suc synthase (Amor et al., 1995). Recent in vitro studies suggest that the initiation of ␤-1,4-glucan synthesis starts with the addition of Glc units to a primer, sitosterol lipid, to form lipid-linked oligosaccharides called sitosterol cellodextrin (Peng et al., 2002). Cellodextrins are then thought to be cleaved from the sitosterol primer probably by a KOR cellulase (Nicol et al., 1998) and further elongated by addition of more Glc molecules to form a long chain of ␤-1,4-glucan (Peng et a...

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“…The exact biochemical activity of each CesA isoform, although speculated upon (Read and Bacic 2002), has not yet been shown experimentally apart from one instance in which yeastexpressed GhCesA1 was able to convert sitosterol-b-glucoside to sitosterol cellodextrins, thus confirming their ability to synthesise (1,4)-b-glucan linkages (Peng et al 2002). The CesA isoforms interact directly and when all three are present, they form higher order oligomeric structures involving homodimers (Kurek et al 2002;Gardiner et al 2003;Atanassov et al 2009). Through the use of tagged CesA proteins, it may now be possible to purify CSCs from detergent-soluble extracts and establish whether any other proteins are permanent components of the complex.…”

Section: Cellulosementioning

confidence: 97%

Plant cell walls: the skeleton of the plant world

Doblin

Pettolino

Bacic

2010

Functional Plant Biol.

182

140

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Abstract. Plants are our major source of renewable biomass. Since cell walls represent some 50% of this biomass, they are major targets for biotechnology. Major drivers are their potential as a renewable source of energy as transport fuels (biofuels), functional foods to improve human health and as a source of raw materials to generate building blocks for industrial processes (biobased industries). To achieve sustainable development, we must optimise plant production and utilisation and this will require a complete understanding of wall structure and function at the molecular/biochemical level. This overview summarises the current state of knowledge in relation to the synthesis and assembly of the wall polysaccharides (i.e. the genes and gene families encoding the polysaccharide synthases and glycosyltransferases (GlyTs)), the predominant macromolecular components. We also touch on an exciting emerging role of the cell wall-plasma membrane-cytoskeleton continuum as a signal perception and transduction pathway allowing plant growth regulation in response to endogenous and exogenous cues.Additional keywords: cell wall-plasma membrane-cytoskeleton continuum, glycosyltransferase, polysaccharide structure and biosynthesis, synthase. Plant cell wallsA distinguishing feature of plant cells is the presence of a polysaccharide-rich wall. The wall encloses each cell while at the same time allowing the transfer of solutes and signalling molecules between cells via specific structures such as plasmodesmata (symplastic transport), or pores within the gellike matrix of the wall itself (apoplastic movement). Similar to the skeleton of animals, the plant wall is a key determinant of overall plant form, growth and development. In contrast to having a specialised skeletal system as occurs in animals, the shape and strength of plants rely on the properties of the wall. The wall also plays a significant role in plant defence and responses to environmental stresses. Plant walls are important not simply because they are integral to plant growth and development but also because they determine the quality of plant-based products. The texture, nutritional and processing properties of plant-based foods for human and animal consumption is heavily influenced by the characteristics of the wall. Fibre for textiles, pulp and paper manufacture, and timber products and increasingly for fuel and composite manufacture is largely composed of walls, or derived from them. Due to their relevance to these industries, the chemical structures of the constituent polymers (polysaccharides, (glyco) proteins, polyphenolics) and the biochemical processes involved in the synthesis, maturation and turnover of the wall have been the subjects of research for many years. This research is now intensifying with the prospect of using plant ligno-cellulosic biomass as a viable and sustainable alternative to fossil fuels in the production of transportation fuels. Advances are likely to occur through molecular biological and functional genomics approaches, including pu...

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Dimerization of cotton fiber cellulose synthase catalytic subunits occurs via oxidation of the zinc-binding domains

Cited by 227 publications

References 36 publications

Knockout of the AtCESA2 Gene Affects Microtubule Orientation and Causes Abnormal Cell Expansion in Arabidopsis

Knockout of the AtCESA2 Gene Affects Microtubule Orientation and Causes Abnormal Cell Expansion in Arabidopsis

Expression of a Mutant Form of Cellulose Synthase AtCesA7 Causes Dominant Negative Effect on Cellulose Biosynthesis

Plant cell walls: the skeleton of the plant world

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