<i>AtCSLD3</i>, A Cellulose Synthase-Like Gene Important for Root Hair Growth in Arabidopsis

Wang, Xuan; Cnops, Gerda; Vanderhaeghen, Rudy; Block, Sabine De; Montagu, Marc Van; Lijsebettens, Mieke Van

doi:10.1104/pp.126.2.575

Cited by 145 publications

(168 citation statements)

References 41 publications

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“…The cellulose synthase-like CSLD3, which is essential for the synthesis of the primary cell wall polymers in fast-growing tissues (Wang et al 2001), and a member of the subgroup A α-expansin family EXPA8 of expansins that are known to allow cell wall enlargements by the disruption of hydrogen bonding between cell wall polymers (McQueen-Mason and Cosgrove 1994), were upregulated in cork oak samples. This observation suggest that the growth of cork cells might involve the synthesis of primary cell wall by CSLD proteins and the extension of cell walls by members of the subgroup A α-expansins, which are both protein families typically found in fast-growing and expanding tissues (Gray-Mitsumune et al 2004;Bernal et al 2008).…”

Section: Discussionmentioning

confidence: 99%

A comparative transcriptomic approach to understanding the formation of cork

et al. 2017

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Key message The transcriptome comparison of two oak species reveals possible candidates accounting for the exceptionally thick and pure cork oak phellem, such as those involved in secondary metabolism and phellogen activity. Abstract Cork oak, Quercus suber, differs from other Mediterranean oaks such as holm oak (Quercus ilex) by the thickness and organization of the external bark. While holm oak outer bark contains sequential periderms interspersed with dead secondary phloem (rhytidome), the cork oak outer bark only contains thick layers of phellem (cork rings) that accumulate until reaching a thickness that allows industrial uses. Here we compare the cork oak outer bark transcriptome with that of holm oak. Both transcriptomes present similitudes in their complexity, but whereas cork oak external bark is enriched with upregulated genes related to suberin, which is the main polymer responsible for the protective function of periderm, the upregulated categories of holm oak are enriched in abiotic stress and chromatin assembly. Concomitantly with the upregulation of suberin-related genes, there is also induction of regulatory and meristematic genes, whose predicted activities agree with the increased number of phellem layers found in the cork oak sample. Further transcript profiling among different cork oak tissues and conditions suggests that cork and wood share many regulatory mechanisms, probably reflecting similar ontogeny. Moreover, the analysis of transcripts accumulation during the cork growth season showed that most regulatory genes are upregulated early in the season when the cork cambium becomes active. Altogether our work provides the first transcriptome comparison between cork oak and holm oak outer bark, which unveils new regulatory candidate genes of phellem development.

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Section: Discussionmentioning

confidence: 99%

A comparative transcriptomic approach to understanding the formation of cork

et al. 2017

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“…Several mutants have been isolated that affect root hair elongation and potentially disrupt these processes (33)(34)(35)(36). Thus, the elongated root hairs of the atipk1-1 plants may result from the aberrant regulation of one of these processes.…”

Section: Discussionmentioning

confidence: 99%

Generation of phytate-free seeds in Arabidopsis through disruption of inositol polyphosphate kinases

Stevenson-Paulik

Bastidas

Chiou

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

276

359

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Phytate (inositol hexakisphosphate, IP6) is a regulator of intracellular signaling, a highly abundant animal antinutrient, and a phosphate store in plant seeds. Here, we report a requirement for inositol polyphosphate kinases, AtIPK1 and AtIPK2␤, for the later steps of phytate synthesis in Arabidopsis thaliana. Coincident disruption of these kinases nearly ablates seed phytate without accumulation of phytate precursors, increases seed-free phosphate by 10-fold, and has normal seed yield. Additionally, we find a requirement for inositol tetrakisphosphate (IP 4)͞inositol pentakisphosphate (IP 5) 2-kinase activity in phosphate sensing and root hair elongation. Our results define a commercially viable strategy for the genetic engineering of phytate-free grain and provide insights into the role of inositol polyphosphate kinases in phosphate signaling biology.genetically engineered crops ͉ low phytate ͉ signal transduction ͉ phosphate sensing

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“…The percentage of inside-out Golgi complex vesicles is determined by comparing the XyG FUTase activity assayed with or without permeabilization of the membrane vesicles with 1% Triton X-100. In this case, the inside-out or unsealed vesicles constitute only 8.8% of the total Wang et al 2001), AtCSLD5 (Bernal et al 2007), and OsCSLD1 (Kim et al 2007). However, none of the mutations have been linked to changes in speciWc sugar linkages within a speciWc cell wall polysaccharide and therefore the biochemical functions of these genes could not be determined from these studies.…”

Section: Discussionmentioning

confidence: 99%

AtCSLD2 is an integral Golgi membrane protein with its N-terminus facing the cytosol

Zeng

Keegstra

2008

Planta

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Cellulose synthase-like proteins in the D family share high levels of sequence identity with the cellulose synthase proteins and also contain the processive -glycosyltransferase motifs conserved among all members of the cellulose synthase superfamily. Consequently, it has been hypothesized that members of the D family function as either cellulose synthases or glycan synthases involved in the formation of matrix polysaccharides. As a prelude to understanding the function of proteins in the D family, we sought to determine where they are located in the cell. A polyclonal antibody against a peptide located at the N-terminus of the Arabidopsis D2 cellulose synthase-like protein was generated and puriWed. After resolving Golgi vesicles from plasma membranes using endomembrane puriWcation techniques including two-phase partitioning and sucrose density gradient centrifugation, we used antibodies against known proteins and marker enzyme assays to characterize the various membrane preparations. The Arabidopsis cellulose synthase-like D2 protein was found mostly in a fraction that was enriched with Golgi membranes. In addition, versions of the Arabidopsis cellulose synthase-like D2 proteins tagged with a green Xuorescent protein was observed to colocalize with a DsRed-tagged Golgi marker protein, the rat alpha-2,6-sialyltransferase. Therefore, we postulate that the majority of Arabidopsis cellulose synthase-like D proteins, under our experimental conditions, are likely located at the Golgi membranes. Furthermore, protease digestion of Golgi-rich vesicles revealed almost complete loss of reaction with the antibodies, even without detergent treatment of the Golgi vesicles. Therefore, the N-terminus of the Arabidopsis cellulose synthase-like D2 protein likely faces the cytosol. Combining this observation with the transmembrane domain predictions, we postulate that the large hydrophilic domain of this protein also faces the cytosol.

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AtCSLD3, A Cellulose Synthase-Like Gene Important for Root Hair Growth in Arabidopsis

Cited by 145 publications

References 41 publications

A comparative transcriptomic approach to understanding the formation of cork

A comparative transcriptomic approach to understanding the formation of cork

Generation of phytate-free seeds in Arabidopsis through disruption of inositol polyphosphate kinases

AtCSLD2 is an integral Golgi membrane protein with its N-terminus facing the cytosol

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