Influence of vesicular trichomes of Atriplex nummularia on photosynthesis, osmotic adjustment, cell wall elasticity and enzymatic activity

2020 ◽  
Vol 155 ◽  
pp. 177-186
Author(s):  
Martha Katharinne Silva Souza Paulino ◽  
Edivan Rodrigues de Souza ◽  
Cíntia Maria Teixeira Lins ◽  
Pablo Rugero Magalhães Dourado ◽  
Lucas Yago de Carvalho Leal ◽  
...  
2010 ◽  
Vol 135 (2) ◽  
pp. 125-133 ◽  
Author(s):  
Qi Chai ◽  
Fang Jin ◽  
Emily Merewitz ◽  
Bingru Huang

The objective of this study was to determine physiological traits for drought survival and post-drought recovery upon re-watering in two C3 perennial grass species, kentucky bluegrass [KBG (Poa pratensis)] and perennial ryegrass [PRG (Lolium perenne)]. Plants were maintained well watered or exposed to drought stress by withholding irrigation and were then re-watered in a growth chamber. KBG had significantly higher grass quality and leaf photochemical efficiency, and lower electrolyte leakage than PRG during 20 days of drought. After 7 days of re-watering, drought-damaged leaves were rehydrated to the control level in KBG, but could not fully recover in PRG. KBG produced a greater number of new roots, while PRG had more rapid elongation of new roots after 16 days of re-watering. Superior drought tolerance in KBG was associated with osmotic adjustment, higher cell wall elasticity, and lower relative water content at zero turgor. Osmotic adjustment, cell wall elasticity, and cell membrane stability could play important roles in leaf desiccation tolerance and drought survival in perennial grass species. In addition, post-drought recovery of leaf hydration level and physiological activity could be associated with the accumulation of carbohydrates in leaves and rhizomes during drought stress and new root production after re-watering.


2020 ◽  
Vol 150 ◽  
pp. 133-139 ◽  
Author(s):  
Hatim Al-Yasi ◽  
Houneida Attia ◽  
Khalid Alamer ◽  
Fahmy Hassan ◽  
Esmat Ali ◽  
...  

2009 ◽  
Vol 67 (2) ◽  
pp. 312-319 ◽  
Author(s):  
Kamel Hessini ◽  
Juan Pablo Martínez ◽  
Mhemmed Gandour ◽  
Ali Albouchi ◽  
Abdelaziz Soltani ◽  
...  

2018 ◽  
pp. 335-347 ◽  
Author(s):  
Thomas Torode ◽  
Marina Linardic ◽  
J. Louis Kaplan ◽  
Siobhan A. Braybrook

1996 ◽  
Vol 17 (2) ◽  
pp. 373-382 ◽  
Author(s):  
J. PENUELAS ◽  
I. FILELLA ◽  
L. SERRANO ◽  
R. SAVÉ

2011 ◽  
Vol 76 (9) ◽  
pp. 1229-1236 ◽  
Author(s):  
Mira Milisavljevic ◽  
Gordana Timotijevic ◽  
Dragana Nikolic ◽  
Jelena Samardzic ◽  
Vesna Maksimovic

The recombinant aspartic proteinase-like protein (FeAPL1-His6) was overexpressed in the tobacco BY-2 cell line and the expected pepstatin A-sensitive enzymatic activity was confirmed at pH 3.0. Immunocytochemistry and protein gel blot analysis of the transformed BY-2 cells and their protoplasts showed extracellular localization of rFeAPL1-His6 in the cell wall. Based on the obtained results, potential functions of FeAPL1 are discussed.


2010 ◽  
Vol 432 (3) ◽  
pp. 557-566 ◽  
Author(s):  
Emily R. Slepkov ◽  
Alan Pavinski Bitar ◽  
Hélène Marquis

The intracellular bacterial pathogen Listeria monocytogenes secretes a broad-range phospholipase C enzyme called PC-PLC (phosphatidylcholine phospholipase C) whose compartmentalization and enzymatic activity is regulated by a 24-amino-acid propeptide (Cys28–Ser51). During intracytosolic multiplication, bacteria accumulate the proform of PC-PLC at their membrane–cell-wall interface, whereas during cell-to-cell spread vacuolar acidification leads to maturation and rapid translocation of PC-PLC across the cell wall in a manner that is dependent on Mpl, the metalloprotease of Listeria. In the present study, we generated a series of propeptide mutants to determine the minimal requirement to prevent PC-PLC enzymatic activity and to identify residues regulating compartmentalization and maturation. We found that a single residue at position P1 (Ser51) of the cleavage site is sufficient to prevent enzymatic activity, which is consistent with P1′ (Trp52) being located within the active-site pocket. We observed that mutants with deletions at the N-terminus, but not the C-terminus, of the propeptide are translocated across the cell wall more effectively than wild-type PC-PLC at a physiological pH, and that individual amino acid residues within the N-terminus influence Mpl-mediated maturation of PC-PLC at acidic pH. However, deletion of more than 75% of the propeptide was required to completely prevent Mpl-mediated maturation of PC-PLC. These results indicate that the N-terminus of the propeptide regulates PC-PLC compartmentalization and that specific residues within the N-terminus influence the ability of Mpl to mediate PC-PLC maturation, although a six-residue propeptide is sufficient for Mpl to mediate PC-PLC maturation.


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