HYDROXYPROLINE-INDUCED CHANGES IN FORM, APICAL DEVELOPMENT, AND CELL WALL PROTEIN IN THE LIVERWORT PLAGIOCHILA ARCTICA

1979 ◽  
Vol 66 (7) ◽  
pp. 776-783 ◽  
Author(s):  
Dominick V. Basile ◽  
Herbert H. Lehman
2016 ◽  
Vol 73 (1) ◽  
pp. 71-81 ◽  
Author(s):  
María S. Escolano-Martínez ◽  
Arnau Domenech ◽  
José Yuste ◽  
María I. Cercenado ◽  
Carmen Ardanuy ◽  
...  

Planta ◽  
2021 ◽  
Vol 253 (5) ◽  
Author(s):  
Peilei Chen ◽  
Valentino Giarola ◽  
Dorothea Bartels

Abstract Main conclusion The cell wall protein CpWAK1 interacts with pectin, participates in decoding cell wall signals, and induces different downstream responses. Abstract Cell wall-associated protein kinases (WAKs) are transmembrane receptor kinases. In the desiccation-tolerant resurrection plant Craterostigma plantagineum, CpWAK1 has been shown to be involved in stress responses and cell expansion by forming a complex with the C. plantagineum glycine-rich protein1 (CpGRP1). This prompted us to extend the studies of WAK genes in C. plantagineum. The phylogenetic analyses of WAKs from C. plantagineum and from other species suggest that these genes have been duplicated after species divergence. Expression profiles indicate that CpWAKs are involved in various biological processes, including dehydration-induced responses and SA- and JA-related reactions to pathogens and wounding. CpWAK1 shows a high affinity for “egg-box” pectin structures. ELISA assays revealed that the binding of CpWAKs to pectins is modulated by CpGRP1 and it depends on the apoplastic pH. The formation of CpWAK multimers is the prerequisite for the CpWAK–pectin binding. Different pectin extracts lead to opposite trends of CpWAK–pectin binding in the presence of Ca2+ at pH 8. These observations demonstrate that CpWAKs can potentially discriminate and integrate cell wall signals generated by diverse stimuli, in concert with other elements, such as CpGRP1, pHapo, Ca2+[apo], and via the formation of CpWAK multimers.


1997 ◽  
Vol 25 (5) ◽  
pp. 345-348 ◽  
Author(s):  
M. Gatti ◽  
E. Fornasari ◽  
E. Neviani

2013 ◽  
Vol 57 (8) ◽  
pp. 3889-3896 ◽  
Author(s):  
Farida Islahudin ◽  
Combiz Khozoie ◽  
Steven Bates ◽  
Kang-Nee Ting ◽  
Richard J. Pleass ◽  
...  

ABSTRACTChloroquine (CQ) has been a mainstay of antimalarial drug treatment for several decades. Additional therapeutic actions of CQ have been described, including some reports of fungal inhibition. Here we investigated the action of CQ in fungi, including the yeast modelSaccharomyces cerevisiae. A genomewide yeast deletion strain collection was screened against CQ, revealing thatbck1Δ andslt2Δ mutants of the cell wall integrity pathway are CQ hypersensitive. This phenotype was rescued with sorbitol, consistent with cell wall involvement. The cell wall-targeting agent caffeine caused hypersensitivity to CQ, as did cell wall perturbation by sonication. The phenotypes were not caused by CQ-induced changes to cell wall components. Instead, CQ accumulated to higher levels in cells with perturbed cell walls: CQ uptake was 2- to 3-fold greater inbck1Δ andslt2Δ mutants than in wild-type yeast. CQ toxicity was synergistic with that of the major cell wall-targeting antifungal drug, caspofungin. The MIC of caspofungin against the yeast pathogenCandida albicanswas decreased 2-fold by 250 μM CQ and up to 8-fold at higher CQ concentrations. Similar effects were seen inCandida glabrataandAspergillus fumigatus. The results show that the cell wall is critical for CQ resistance in fungi and suggest that combination treatments with cell wall-targeting drugs could have potential for antifungal treatment.


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