scholarly journals Comparison and Characterization of a Cell Wall Invertase Promoter from Cu-Tolerant and Non-Tolerant Populations of Elsholtzia haichowensis

2021 ◽  
Vol 22 (10) ◽  
pp. 5299
Author(s):  
Rongxiang Liu ◽  
Jing Zhao ◽  
Zhongrui Xu ◽  
Zhiting Xiong
Keyword(s):  
Cell Wall ◽  
Copper Stress ◽  
Cell Wall Invertase ◽  
Gus Reporter ◽  
Elsholtzia Haichowensis ◽  
Population Comparison ◽  
A Cell ◽  
Two Populations

Cell wall invertase (CWIN) activity and the expression of the corresponding gene were previously observed to be significantly elevated in a Cu-tolerant population of Elsholtzia haichowensis relative to a non-tolerant population under copper stress. To understand the differences in CWIN gene regulation between the two populations, their CWIN promoter β-glucuronidase (GUS) reporter vectors were constructed. GUS activity was measured in transgenic Arabidopsis in response to copper, sugar, and phytohormone treatments. Under the copper treatment, only the activity of the CWIN promoter from the Cu-tolerant population was slightly increased. Glucose and fructose significantly induced the activity of CWIN promoters from both populations. Among the phytohormone treatments, only salicylic acid induced significantly higher (p < 0.05) activity of the Cu-tolerant CWIN promoter relative to the non-tolerant promoters. Analysis of 5′-deletion constructs revealed that a 270-bp promoter fragment was required for SA induction of the promoter from the Cu-tolerant population. Comparison of this region in the two CWIN promoters revealed that it had 10 mutation sites and contained CAAT-box and W-box cis-elements in the Cu-tolerant promoter only. This work provides insights into the regulatory role of SA in CWIN gene expression and offers an explanation for differences in CWIN expression between E. haichowensis populations.

cDNA cloning, heterologous expression and characterization of a cell wall invertase from copper tolerant population of Elsholtzia haichowensis

Biologia ◽  
2015 ◽  
Vol 70 (8) ◽  
Author(s):  
Chen Liu ◽  
Zhongrui Xu ◽  
Shenwen Cai ◽  
Luan Zhang ◽  
Zhiting Xiong
Keyword(s):  
Cell Wall ◽  
Evolutionary Relationship ◽  
Methylotrophic Yeast ◽  
Cell Wall Invertase ◽  
Reading Frame ◽  
Methylotrophic Yeast Pichia Pastoris ◽  
Acid Protein ◽  
Elsholtzia Haichowensis ◽  
A Cell ◽  
Theoretical Molecular Mass

AbstractThe main objective of the present study was to clone, heterologously express and characterize a novel cell wall invertase (FCWI) from a Cu tolerant population of Elsholtzia haichowensis. The full-length FCWI cDNA contained an open reading frame (ORF) of 1671 bp which encoded a 556-amino-acid protein. The theoretical molecular mass and pI of the deduced protein were 62.5 kDa and 9.29, respectively. Phylogenetic analysis showed that FCWI had a closer evolutionary relationship to cell wall invertase of dicot. FCWI was expressed in methylotrophic yeast Pichia pastoris and purified to near homogeneity. Recombinant FCWI enzyme had pH optima of 4.0 and temperature optima of 50◦C. Activity analyses in the presence of various metal cations indicated that FCWI was completely inhibited by Hg

scholarly journals Physiological function of Flo11p domains and the particular role of amyloid core sequences of this adhesin in Saccharomyces cerevisiae

2021 ◽  
Author(s):  
Clara Bouyx ◽  
Marion Schiavone ◽  
Marie-Ange Teste ◽  
Etienne Dague ◽  
Nathalie Sieczkowski ◽  
...  
Keyword(s):  
Cell Wall ◽  
Amyloid Β ◽  
Surface Hydrophobicity ◽  
Yeast Cells ◽  
Invasive Growth ◽  
Specific Domain ◽  
A Genome ◽  
A Cell ◽  
Cellular Aggregates

Flocculins are a family of glycosylated proteins that provide yeast cells with several properties such as biofilm formation, flocculation, invasive growth or formation of velum. These proteins are similarly organised with a N-terminal (adhesion) domain, a stalk-like central B-domain with several repeats and a C-terminal sequence carrying a cell wall anchor site. They also contain amyloid β-aggregation-prone sequences whose functional role is still unclear. In this work, we show that Flo11p differs from other flocculins by the presence of unique amyloid-forming sequences, whose the number is critical in the formation of adhesion nanodomains under a physical shear force. Using a genome editing approach to identify the function of domains in Flo11p phenotypes, we show that the formation of cellular aggregates whose density increases with the number of amyloid sequences cannot be attributed to a specific domain of Flo11p. The same is true for plastic adhesion and surface hydrophobicity the intensity of which depends mainly on the abundance of Flo11p on the cell surface. In contrast, the N and C domains of Flo11p are essential for invasive growth in agar, whereas a reduction in the number of repeats of the B domain weakens this phenotype. However, expression of FLO11 alone is not sufficient to trigger this invasion phenotype. Finally, we show that this flocculin contributes to the integrity of the cell wall.

Isolation and first characterization of a cell-wall-degrading agent of Chlorella

1979 ◽  
Vol 66 (10) ◽  
pp. 525-526 ◽  
Author(s):  
G. Touet ◽  
H. G. Aach
Keyword(s):  
Cell Wall ◽  
A Cell

The role of Golgi bodies in polysaccharide sulphation in Fucuszygotes

1978 ◽  
Vol 32 (1) ◽  
pp. 337-356
Author(s):  
M.E. Callow ◽  
S.J. Coughlan ◽  
L.V. Evans
Keyword(s):  
Cell Wall ◽  
Alginic Acid ◽  
Soluble Fraction ◽  
Amorphous Layer ◽  
Acceptor Molecule ◽  
Golgi Bodies ◽  
Isolation And Characterization ◽  
Fucus Serratus

The cell wall of 24-h zygotes of Fucus serratus is composed of 3 layers—an inner fibrillar layer (sulphated fucan), an outer fibrillar layer (alginic aicd/cellulose) and an exterior amorphous layer (sulphated fucan, alginic acid). The 2 layers containing sulphated fucan are preferentially thickened at the rhizoid pole. Light- and electron-microscope autoradiographic pulse-chase experiments on 22-h zygotes using 35SO2-(4) show the Golgi bodies to be the sites of fucan sulphation. The isolation and characterization of isolated Golgi-rich fractions from 22-h zygotes shows that the first detectable labelled macromolecule is associated with these fractions 2 min after addition of 35SO2-(4). The sulphate acceptor molecule has been partially characterized. 35S-APS and 35S-paps are detectable in the soluble fraction 0.5 min after addition of 35SO2-(4). The results are discussed in relation to other published work on the differentiation of Fucus embryos and on polysaccharide sulphation.

scholarly journals The Epigenetic Repertoire of Daphnia magna Includes Modified Histones

2012 ◽  
Vol 2012 ◽  
pp. 1-7 ◽  
Author(s):  
Nicole F. Robichaud ◽  
Jeanette Sassine ◽  
Margaret J. Beaton ◽  
Vett K. Lloyd
Keyword(s):  
Life Cycle ◽  
Histone H3 ◽  
Dependent Manner ◽  
Nurse Cells ◽  
Important Species ◽  
Clonal Population ◽  
A Cell ◽  
Cycle Dependent

Daphnids are fresh water microcrustaceans, many of which follow a cyclically parthenogenetic life cycle. Daphnia species have been well studied in the context of ecology, toxicology, and evolution, but their epigenetics remain largely unexamined even though sex determination, the production of sexual females and males, and distinct adult morphological phenotypes, are determined epigenetically. Here, we report on the characterization of histone modifications in Daphnia. We show that a number of histone H3 and H4 modifications are present in Daphnia embryos and histone H3 dimethylated at lysine 4 (H3K4me2) is present nonuniformly in the nucleus in a cell cycle-dependent manner. In addition, this histone modification, while present in blastula and gastrula cells as well as the somatic cells of adults, is absent or reduced in oocytes and nurse cells. Thus, the epigenetic repertoire of Daphnia includes modified histones and as these epigenetic forces act on a genetically homogeneous clonal population Daphnia offers an exceptional tool to investigate the mechanism and role of epigenetics in the life cycle and development of an ecologically important species.

scholarly journals First Structural Characterization of a Bon-Domain in a Protein from Mycobacterium Tuberculosis: OmpATb Tracks toward an Oligomerization Process to form a Cell Wall Pore

2010 ◽  
Vol 98 (3) ◽  
pp. 648a
Author(s):  
Daniel Auguin ◽  
Yinshan Yang ◽  
Stephane Delbecq ◽  
Emilie Dumas ◽  
Virginie Molle ◽  
...  
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Structural Characterization ◽  
A Cell
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