Quantifying plant cell-wall failure in vivo using nanoindentation

2014 ◽  
Vol 4 (3) ◽  
pp. 107-111 ◽  
Author(s):  
Elham Forouzesh ◽  
Ashwani K. Goel ◽  
Joseph A. Turner
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Image Position

Abstract

scholarly journals Oxidative scission of plant cell wall polysaccharides by ascorbate-induced hydroxyl radicals

1998 ◽  
Vol 332 (2) ◽  
pp. 507-515 ◽  
Author(s):  
Stephen C. FRY
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Hydroxyl Radicals ◽  
Plant Cell Wall ◽  
Oh Radicals ◽  
Radical Scavengers ◽  
Cell Wall Polysaccharides ◽  
Ph Optimum ◽  
Living Plant

Scission of plant cell wall polysaccharides in vivo has generally been assumed to be enzymic. However, in the presence of l-ascorbate, such polysaccharides are shown to undergo non-enzymic scission under physiologically relevant conditions. Scission of xyloglucan by 1 mM ascorbate had a pH optimum of 4.5, and the maximum scission rate was reached after a 10–25-min delay. Catalase prevented the scission, whereas added H2O2 (0.1–10 mM) increased the scission rate and shortened the delay. Ascorbate caused detectable xyloglucan scission above approx. 5 µM. Dehydroascorbate was much less effective. Added Cu2+ (> 0.3 µM) also increased the rate of ascorbate-induced scission; EDTA was inhibitory. The rate of scission in the absence of added metals appeared to be attributable to the traces of Cu (2.8 mg·kg-1) present in the xyloglucan. Ascorbate-induced scission of xyloglucan was inhibited by radical scavengers; their effectiveness was proportional to their rate constants for reaction with hydroxyl radicals (•OH). It is proposed that ascorbate non-enzymically reduces O2 to H2O2, and Cu2+ to Cu+, and that H2O2 and Cu+ react to form •OH, which causes oxidative scission of polysaccharide chains. Evidence is reviewed to suggest that, in the wall of a living plant cell, Cu+ and H2O2 are formed by reactions involving ascorbate and its products, dehydroascorbate and oxalate. Systems may thus be in place to produce apoplastic •OH radicals in vivo. Although •OH radicals are often regarded as detrimental, they are so short-lived that they could act as site-specific oxidants targeted to play a useful role in loosening the cell wall, e.g. during cell expansion, fruit ripening and organ abscission.

scholarly journals Di-isodityrosine, a novel tetrametric derivative of tyrosine in plant cell wall proteins: a new potential cross-link

1996 ◽  
Vol 315 (1) ◽  
pp. 323-327 ◽  
Author(s):  
Jeffrey D. BRADY ◽  
Ian H. SADLER ◽  
Stephen C. FRY
Keyword(s):  
Cell Culture ◽  
Cell Wall ◽  
Amino Acid ◽  
Plant Cell ◽  
Cell Walls ◽  
Plant Cell Wall ◽  
Cell Wall Proteins ◽  
Cross Link ◽  
Nmr Spectrometry

A novel amino acid, di-isodityrosine, has been isolated from hydrolysates of cell walls of tomato cell culture. Analysis by UV spectrometry, partial derivatization with 2,4-dinitrofluorobenzene and mass and NMR spectrometry show that the compound is composed to two molecules of isodityrosine, joined by a biphenyl linkage. The possible reactions involved in the formation of this molecule in vivo are discussed, as is the possibility that it could form an interpolypeptide linkage between cell wall proteins such as extensin, and hence aid in the insolubilization of the protein in the wall.

One, Two, Three: A Bioorthogonal Triple Labelling Strategy for Studying the Dynamics of Plant Cell Wall Formation In Vivo

2018 ◽  
Vol 130 (51) ◽  
pp. 16907-16913 ◽  
Author(s):  
Clemence Simon ◽  
Cedric Lion ◽  
Corentin Spriet ◽  
Fabien Baldacci‐Cresp ◽  
Simon Hawkins ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Cell Wall Formation ◽  
Wall Formation

A click chemistry strategy for visualization of plant cell wall lignification

2014 ◽  
Vol 50 (82) ◽  
pp. 12262-12265 ◽  
Author(s):  
Yuki Tobimatsu ◽  
Dorien Van de Wouwer ◽  
Eric Allen ◽  
Robert Kumpf ◽  
Bartel Vanholme ◽  
...  
Keyword(s):  
Cell Wall ◽  
Click Chemistry ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Chemical Reporter

Monolignol mimics bearing chemical reporter tags and bioorthogonal click chemistry were commissioned to visualize plant cell wall lignins in vivo.

scholarly journals Enzyme-assisted in vivo polymerisation of conjugated oligomer based conductors

2020 ◽  
Vol 8 (19) ◽  
pp. 4221-4227 ◽  
Author(s):  
Gwennaël Dufil ◽  
Daniela Parker ◽  
Jennifer Y. Gerasimov ◽  
Thuc-Quyen Nguyen ◽  
Magnus Berggren ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Plant Structure

The conjugated oligomer ETE-S is enzymatically polymerized in vitro, in the presence of peroxidase and H2O2. This polymerization route occurs also in the plant cell wall where ETE-S polymerizes and forms conductors along the plant structure.

One, Two, Three: A Bioorthogonal Triple Labelling Strategy for Studying the Dynamics of Plant Cell Wall Formation In Vivo

2018 ◽  
Vol 57 (51) ◽  
pp. 16665-16671 ◽  
Author(s):  
Clemence Simon ◽  
Cedric Lion ◽  
Corentin Spriet ◽  
Fabien Baldacci‐Cresp ◽  
Simon Hawkins ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Cell Wall Formation ◽  
Wall Formation

scholarly journals A role for the Rcs phosphorelay in regulating expression of plant cell wall degrading enzymes in Pectobacterium carotovorum subsp. carotovorum

Microbiology ◽  
2010 ◽  
Vol 156 (5) ◽  
pp. 1323-1334 ◽  
Author(s):  
Liis Andresen ◽  
Erki Sala ◽  
Viia Kõiv ◽  
Andres Mäe
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Pathogenic Bacteria ◽  
Plant Cell Wall ◽  
Response Regulator ◽  
Pectobacterium Carotovorum ◽  
Cell Wall Degrading Enzymes ◽  
Degrading Enzymes ◽  
Direct Binding

The Rcs phosphorelay is a signal transduction system that influences the virulence phenotype of several pathogenic bacteria. In the plant pathogen Pectobacterium carotovorum subsp. carotovorum (Pcc) the response regulator of the Rcs phosphorelay, RcsB, represses expression of plant cell wall degrading enzymes (PCWDE) and motility. The focus of this study was to identify genes directly regulated by the binding of RcsB that also regulate expression of PCWDE genes in Pcc. RcsB-binding sites within the regulatory regions of the flhDC operon and the rprA and rsmB genes were identified using DNase I protection assays, while in vivo studies using flhDC : : gusA, rsmB : : gusA and rprA : : gusA gene fusions revealed gene regulation. These experiments demonstrated that the operon flhDC, a flagellar master regulator, was repressed by RcsB, and transcription of rprA was activated by RcsB. Regulation of the rsmB promoter by RcsB is more complicated. Our results show that RcsB represses rsmB expression mainly through modulating flhDC transcription. Neverthless, direct binding of RcsB on the rsmB promoter region is possible in certain conditions. Using an rprA-negative mutant, it was further demonstrated that RprA RNA is not essential for regulating expression of PCWDE under the conditions tested, whereas overexpression of rprA increased protease expression in wild-type cells. Stationary-phase sigma factor, RpoS, is the only known target gene for RprA RNA in Escherichia coli; however, in Pcc the effect of RprA RNA was found to be rpoS-independent. Overall, our results show that the Rcs phosphorelay negatively affects expression of PCWDE by inhibiting expression of flhDC and rsmB.

scholarly journals Isodityrosine, a new cross-linking amino acid from plant cell-wall glycoprotein

1982 ◽  
Vol 204 (2) ◽  
pp. 449-455 ◽  
Author(s):  
S C Fry
Keyword(s):  
Cell Wall ◽  
Amino Acid ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Higher Plants ◽  
Diphenyl Ether ◽  
Covalent Binding ◽  
Sodium Dodecyl ◽  
Ether Bridge

1. Cell-wall hydrolysates from calli of all higher plants tested contained a new phenolic amino acid for which the trivial name isodityrosine is proposed. Isodityrosine was shown to be an oxidatively coupled dimer of tyrosine with the two tyrosine units linked by a diphenyl ether bridge. 2. The amount of isodityrosine in sodium dodecyl sulphate-insoluble cell-wall preparations was proportional to the amount of hydroxyproline. 3. Acidified chlorite split the diphenyl ether bridge of isodityrosine, and concomitantly solubilized the cell-wall glycoprotein. 4. Dithiothreitol inhibited isodityrosine synthesis in vivo, and suppressed in parallel the covalent binding of newly synthesized protein in the cell wall. 5. It is suggested that isodityrosine is an inter-polypeptide cross-link responsible for the insolubility of plant cell-wall glycoprotein.

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