Ethylene regulation of β-1,3-glucanase in tobacco

Felix, Georg; Meins, Frederick

doi:10.1007/bf00398668

Cited by 84 publications

(45 citation statements)

References 24 publications

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“…They showed sequence similarity with Arabidopsis genes encoding proteins with endomembrane, vacuolar, and/or cell wall localization (e.g., BG1-3; see Bayer et al, 2006) and include the so-called pathogenesis-related group (PR-2) of GH17 proteins (Dong et al, 1991;Uknes et al, 1992). In addition, the LB-related sequences of P. trichocarpa showed similarity to ethylene-and salicylic acid-inducible GH17 enzymes in tobacco (Nicotiana tabacum; Felix and Meins, 1987;Leubner-Metzger et al, 1998). Based on LB association ( Figure 4) and expression patterns during dormancy cycling ( Figure 5), we refer to these g-clade Populus orthologs as group 2 GH17 proteins.…”

Section: Dormancy Release By Chilling Is Related To Effects Of Ga 4 Amentioning

confidence: 99%

Chilling of Dormant Buds HyperinducesFLOWERING LOCUS Tand Recruits GA-Inducible 1,3-β-Glucanases to Reopen Signal Conduits and Release Dormancy inPopulus

et al. 2011

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In trees, production of intercellular signals and accessibility of signal conduits jointly govern dormancy cycling at the shoot apex. We identified 10 putative cell wall 1,3-b-glucanase genes (glucan hydrolase family 17 [GH17]) in Populus that could turn over 1,3-b-glucan (callose) at pores and plasmodesmata (PD) and investigated their regulation in relation to FT and CENL1 expression. The 10 genes encode orthologs of Arabidopsis thaliana BG_ppap, a PD-associated glycosylphosphatidylinositol (GPI) lipid-anchored protein, the Arabidopsis PD callose binding protein PDCB, and a birch (Betula pendula) putative lipid body (LB) protein. We found that these genes were differentially regulated by photoperiod, by chilling (58C), and by feeding of gibberellins GA 3 and GA 4 . GA 3 feeding upregulated all LB-associated GH17s, whereas GA 4 upregulated most GH17s with a GPI anchor and/or callose binding motif, but only GA 4 induced true bud burst. Chilling upregulated a number of GA biosynthesis and signaling genes as well as FT, but not CENL1, while the reverse was true for both GA 3 and GA 4 . Collectively, the results suggest a model for dormancy release in which chilling induces FT and both GPI lipid-anchored and GA 3 -inducible GH17s to reopen signaling conduits in the embryonic shoot. When temperatures rise, the reopened conduits enable movement of FT and CENL1 to their targets, where they drive bud burst, shoot elongation, and morphogenesis.

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Section: Dormancy Release By Chilling Is Related To Effects Of Ga 4 Amentioning

confidence: 99%

Chilling of Dormant Buds HyperinducesFLOWERING LOCUS Tand Recruits GA-Inducible 1,3-β-Glucanases to Reopen Signal Conduits and Release Dormancy inPopulus

et al. 2011

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“…Ethylene is thought to be the natural mediator ofPR protein accumulation (9,25,28,32) as has been found for other defense functions. Physiological stresses that are associated with ethylene, such as flowering (12) and aberrant hormonal levels (8,21), induce synthesis of PR proteins.…”

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confidence: 95%

Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Lotan¹,

Fluhr²

1990

Plant Physiol.

139

103

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Antisera to acidic isoforms of pathogenesis-related proteins were used to measure the induction of these proteins in tobacco (Nicotiana tabacum) leaves. Endo-(1-4)-i-xylanase purified from culture filtrates of Trichoderma viride was a strong elicitor of pathogenesis-related protein synthesis in tobacco leaves. The synthesis of these proteins was localized to tissue at the area of enzyme application. The inhibitors of ethylene biosynthesis and ethylene action, 1-aminoethoxyvinylglycine and silver thiosulfate, inhibited accumulation of pathogenesis-related proteins induced by tobacco mosaic virus and a-aminobutyric acid, but did not inhibit elicitation by xylanase. Likewise, the induction of these proteins by the tobacco pathogen Pseudomonas syringae pv. tabaci was not affected by the inhibitors of ethylene biosynthesis and action. The leaf response to tobacco mosaic virus and aaminobutyric acid was dependent on light in normal and photosynthetically incompetent leaves. In contrast, the response of leaves to xylanase was independent of light. Tobacco mosaic virus and a-aminobutyric acid induced concerted accumulation of pathogenesis-related proteins. However, xylanase elicited the accumulation of only a subset of these proteins. Specifically, the plant (1-3)-,6-glucanases, which are normally a part of the concerted response, were underrepresented. These experiments have revealed the presence of a novel ethylene-independent pathway for pathogenesis-related protein induction that is activated by xylanase.The de novo synthesis of PR2 proteins is a ubiquitous reaction of monocot (10,23,33)

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“…These enzymes also can be found in specialized tissue types such as the leaf epidermis ( 11) and in stylar tissues of the flower (15). In cultured tobacco cells, basic A-1,3-glucanases and their mRNAs are down-regulated by combinations of the growth hormones auxin and cytokinin (7,18) and are induced both in culture and in intact plants by the stress hormone ethylene (8).…”

mentioning

confidence: 99%

Differential Regulation of β-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection

Ward¹,

Payne²,

Moyer³

et al. 1991

Plant Physiol.

146

101

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The acidic, extracellular, glucan endo-1,3-t8-glucosidases (EC 3.2.1.39; j0-1,3-glucanases), pathogenesis-related proteins-2, -N, and -O (i.e. PR-2, PR-N, and PR-0) were purified from Nicotiana tabacum (tobacco) and their partial amino acid sequences determined. Based on these data, complementary DNA (cDNA) clones encoding the proteins were isolated. Additional cDNAs were isolated that encoded proteins approximately 90% identical with PR-2, PR-N, and PR-0. Although the proteins encoded by these cDNAs have not been identified, their deduced amino acid sequences have slightly basic or neutral calculated isoelectric points, as well as carboxy-terminal extensions. These physical characteristics are shared by the vacuolar form of ,B-1,3-glucanase and other vacuolar localized analogs of PR proteins, suggesting that the unidentified proteins may be similarly localized.A preliminary evolutionary model that separates the fl-1,3-glucanase gene family from tobacco into at least five distinct subfamilies is proposed. The expression of ,-1,3-glucanase messenger RNAs (mRNAs) in response to infection by tobacco mosaic virus was examined. Messages for the acidic glucanases were induced similarly to the mRNAs for other PR proteins. However, the basic glucanase showed a different response, suggesting that different isoforms are differentially regulated by tobacco mosaic virus infection at the mRNA level.

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Ethylene regulation of β-1,3-glucanase in tobacco

Cited by 84 publications

References 24 publications

Chilling of Dormant Buds HyperinducesFLOWERING LOCUS Tand Recruits GA-Inducible 1,3-β-Glucanases to Reopen Signal Conduits and Release Dormancy inPopulus

Chilling of Dormant Buds HyperinducesFLOWERING LOCUS Tand Recruits GA-Inducible 1,3-β-Glucanases to Reopen Signal Conduits and Release Dormancy inPopulus

Xylanase, a Novel Elicitor of Pathogenesis-Related Proteins in Tobacco, Uses a Non-Ethylene Pathway for Induction

Differential Regulation of β-1,3-Glucanase Messenger RNAs in Response to Pathogen Infection

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