Cell Wall Genomics in the Recombinogenic Moss Physcomitrella patens

Lawton, Michael; Saidasan, Hemalatha

doi:10.1007/978-0-387-92740-4_14

Cited by 5 publications

(4 citation statements)

References 53 publications

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“…Given that extensins are heavily hydroxyproline O ‐arabinosylated and function in the cell wall (Velasquez et al ., ), these proteins would be the likely targets for HPAT modification in protonema. However, the Physcomitrella genome is unusual among plants in that it does not encode canonical extensins (Lawton and Saidasan, ). In the absence of canonical extensins, we searched the Physcomitrella genome for genes encoding the extensin glycosylation motif and found 20 predicted extensin chimeras containing three or more Ser(Pro) 3 motifs (Table S2).…”

Section: Resultsmentioning

confidence: 99%

“…Third, the HPATs, as members of glycosyltransferase superfamily, will exert their effects through the proteins they target for modification. Despite the lack of canonical extensins (Lawton and Saidasan, ), the Physcomitrella genome encodes not only the HPATs, members of the GT8 glycosyltransferase family (Nikolovski et al ., , Carbohydrate Active enZYmes Database; http://www.cazy.org/), but also all known glycosyltransferases associated with extensin modification including the later‐acting arabinosyltransferases of the GT77 family, RRA1‐3 and XEG113 (Egelund et al ., ; Gille et al ., ; Velasquez et al ., ; Harholt et al ., ). Serine in the Ser(Hyp) 4 context is also modified with a single galactose by SGT1 (Lamport et al ., ; Saito et al ., ), two homologs of which are encoded in the Physcomitrella genome.…”

Section: Discussionmentioning

confidence: 99%

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Hydroxyproline O‐arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens

et al. 2015

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SummaryHydroxyproline O‐arabinosyltransferases (HPATs) are members of a small, deeply conserved family of plant‐specific glycosyltransferases that add arabinose sugars to diverse proteins including cell wall‐associated extensins and small signaling peptides. Recent genetic studies in flowering plants suggest that different HPAT homologs have been co‐opted to function in diverse species‐specific developmental contexts. However, nothing is known about the roles of HPATs in basal plants. We show that complete loss of HPAT function in Arabidopsis thaliana and the moss Physcomitrella patens results in a shared defect in gametophytic tip cell growth. Arabidopsis hpat1/2/3 triple knockout mutants suffer from a strong male sterility defect as a consequence of pollen tubes that fail to fully elongate following pollination. Knocking out the two HPAT genes of Physcomitrella results in larger multicellular filamentous networks due to increased elongation of protonemal tip cells. Physcomitrella hpat mutants lack cell‐wall associated hydroxyproline arabinosides and can be rescued with exogenous cellulose, while global expression profiling shows that cell wall‐associated genes are severely misexpressed, implicating a defect in cell wall formation during tip growth. Our findings point to a major role for HPATs in influencing cell elongation during tip growth in plants.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Hydroxyproline O‐arabinosyltransferase mutants oppositely alter tip growth in Arabidopsis thaliana and Physcomitrella patens

et al. 2015

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“…This lack of specialization for extreme conditions combined with abundant genomic resources ( Rensing et al, 2008 ), efficient production of transgenic genotypes, and ease of culture and experimental manipulation ( Cove, 2005 ) provides an opportunity to relate the diversification of gene families to innovations in cell wall composition, structure, and development that accompanied the adaptation of plants to life on land. Other advantages of P. patens include the ability to produce large amounts of tissue consisting of a single cell type (chloronemal filaments) and rapid cell wall regeneration in protoplasts ( Lee et al, 2005a ; Lawton and Saidasan, 2011 ; Roberts et al, 2011 ).…”

Section: Physcomitrella Patens the Model Moss Speciesmentioning

confidence: 99%

“…Extensin was weakly detected in P. patens by CoMPP. Genome searches identified homologs of GT77 proteins implicated in extensin glycosylation ( Harholt et al, 2012 ), but not extensin itself ( Lawton and Saidasan, 2011 ). However, a comprehensive analysis of cell wall protein genes in P. patens has not been reported.…”

Section: Cell Wall Analysismentioning

confidence: 99%

Moss cell walls: structure and biosynthesis

Roberts¹,

Roberts²,

Haigler³

2012

Front. Plant Sci.

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The genome sequence of the moss Physcomitrella patens has stimulated new research examining the cell wall polysaccharides of mosses and the glycosyl transferases that synthesize them as a means to understand fundamental processes of cell wall biosynthesis and plant cell wall evolution. The cell walls of mosses and vascular plants are composed of the same classes of polysaccharides, but with differences in side chain composition and structure. Similarly, the genomes of P. patens and angiosperms encode the same families of cell wall glycosyl transferases, yet, in many cases these families have diversified independently in each lineage. Our understanding of land plant evolution could be enhanced by more complete knowledge of the relationships among glycosyl transferase functional diversification, cell wall structural and biochemical specialization, and the roles of cell walls in plant adaptation. As a foundation for these studies, we review the features of P. patens as an experimental system, analyses of cell wall composition in various moss species, recent studies that elucidate the structure and biosynthesis of cell wall polysaccharides in P. patens, and phylogenetic analysis of P. patens genes potentially involved in cell wall biosynthesis.

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