scholarly journals Asymmetric redundancy of ZERZAUST and ZERZAUST HOMOLOG in different accessions of Arabidopsis thaliana

2018 ◽  
Author(s):  
Prasad Vaddepalli ◽  
Lynette Fulton ◽  
Kay Schneitz
Keyword(s):  
Cell Wall ◽  
Expression Patterns ◽  
Residual Activity ◽  
Duplicate Genes ◽  
Compensation Mechanism ◽  
Evolutionary Innovation ◽  
Gene Contribution ◽  
A Cell ◽  
Close Homolog

AbstractDivergence among duplicate genes is one of the important sources of evolutionary innovation. But, the contribution of duplicate divergence to variation in Arabidopsis accessions is sparsely known. Recently, we studied the role of a cell wall localized protein, ZERZAUST (ZET), in Landsberg erecta (Ler) accession. Here, we present the study of ZET in Columbia (Col) accession, which not only showed differential expression patterns in comparison to Ler, but also revealed its close homolog, ZERZAUST HOMOLOG (ZETH). Although, genetic analysis implied redundancy, expression analysis revealed divergence, with ZETH showing minimal expression in both Col and Ler. In addition, ZETH shows relatively higher expression levels in Col compared to Ler. Our data also reveal compensatory up-regulation of ZETH in Col, but not in Ler, implying it is perhaps dispensable in Ler. However, a novel CRISPR/Cas9-induced zeth allele confirmed that ZETH has residual activity in Ler. The results provide genetic evidence for accession-specific differences in compensation mechanism and asymmetric gene contribution. Thus, our work reveals a novel example for how weakly expressed homologs contribute to diversity among accessions.

scholarly journals Lessons on fruiting body morphogenesis from genomes and transcriptomes of Agaricomycetes

2021 ◽  
Author(s):  
Laszlo G Nagy ◽  
Peter Jan Vonk ◽  
Markus Kunzler ◽  
Csenge Foldi ◽  
Mate Viragh ◽  
...  
Keyword(s):  
Cell Wall ◽  
Fruiting Body ◽  
Expression Patterns ◽  
Schizophyllum Commune ◽  
Gene Families ◽  
Second Phase ◽  
Fruiting Bodies ◽  
Body Development ◽  
Fruiting Body Development

Fruiting bodies of mushroom-forming fungi (Agaricomycetes) are among the most complex structures produced by fungi. Unlike vegetative hyphae, fruiting bodies grow determinately and follow a genetically encoded developmental program that orchestrates tissue differentiation, growth and sexual sporulation. In spite of more than a century of research, our understanding of the molecular details of fruiting body morphogenesis is limited and a general synthesis on the genetics of this complex process is lacking. In this paper, we aim to comprehensively identify conserved genes related to fruiting body morphogenesis and distill novel functional hypotheses for functionally poorly characterized genes. As a result of this analysis, we report 921 conserved developmentally expressed gene families, only a few dozens of which have previously been reported in fruiting body development. Based on literature data, conserved expression patterns and functional annotations, we provide informed hypotheses on the potential role of these gene families in fruiting body development, yielding the most complete description of molecular processes in fruiting body morphogenesis to date. We discuss genes related to the initiation of fruiting, differentiation, growth, cell surface and cell wall, defense, transcriptional regulation as well as signal transduction. Based on these data we derive a general model of fruiting body development, which includes an early, proliferative phase that is mostly concerned with laying out the mushroom body plan (via cell division and differentiation), and a second phase of growth via cell expansion as well as meiotic events and sporulation. Altogether, our discussions cover 1480 genes of Coprinopsis cinerea, and their orthologs in Agaricus bisporus, Cyclocybe aegerita, Armillaria ostoyae, Auriculariopsis ampla, Laccaria bicolor, Lentinula edodes, Lentinus tigrinus, Mycena kentingensis, Phanerochaete chrysosporium, Pleurotus ostreatus, and Schizophyllum commune, providing functional hypotheses for ~10% of genes in the genomes of these species. Although experimental evidence for the role of these genes will need to be established in the future, our data provide a roadmap for guiding functional analyses of fruiting related genes in the Agaricomycetes. We anticipate that the gene compendium presented here, combined with developments in functional genomics approaches will contribute to uncovering the genetic bases of one of the most spectacular multicellular developmental processes in fungi. Key words: functional annotation; comparative genomics; cell wall remodeling; development; fruiting body morphogenesis; mushroom; transcriptome

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.

scholarly journals A Biophysical Model for Plant Cell Plate Development

2020 ◽  
Author(s):  
Muhammad Zaki Jawaid ◽  
Rosalie Sinclair ◽  
Daniel Cox ◽  
Georgia Drakakaki
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Late Stage ◽  
Cell Plate ◽  
Biophysical Model ◽  
Synthesis Rate ◽  
Spontaneous Curvature ◽  
Two Dimensional ◽  
A Cell

AbstractPlant cytokinesis, a fundamental process of plant life, involves de novo formation of a ‘cell plate’ that partitions the cytoplasm of the dividing cell. Cell plate formation is directed by orchestrated delivery, fusion of cytokinetic vesicles, and membrane maturation to the form the nascent cell wall by the timely deposition of polysaccharides such as callose, cellulose, and crosslinking glycans. In contrast to the role of endomembrane protein regulators the role of polysaccharides, in cell plate development is poorly understood. Callose, a β-1-3 glucan polymer, is transiently accumulated during cell plate expansion to be replaced by cellulose in mature stages. Based on the severity of cytokinesis defects in the absence of callose, it has been proposed that it stabilizes this membrane network structure. However, there is currently no theory to understand its role in cytokinesis.Here we extend the Helfrich free energy model for membranes including a phenomenological spreading force as an “areal pressure” generated by callose and/or other polysaccharides. Regular cell plate development in the model is possible, with suitable bending modulus, for a two-dimensional late stage spreading force parameter of between 2–6pN/nm, an osmotic pressure difference of 2–10kPa, and spontaneous curvature between 0–0.04nm−1. With these conditions, stable membrane conformation sizes and morphologies emerge in concordance with stages of cell plate development. With no spreading force, the cell plate fails to mature properly, corroborating experimental observations of cytokinesis arrest in the absence of callose. To reach a nearly mature cell plate, our model requires the late stage onset that the spreading force coupled with a concurrent loss of spontaneous curvature. A simple model based upon production of callose as a quasi-two-dimensional self-avoiding polymer produces the correct phenomenological form of the spreading force, which will be further refined, since matching to our numbers requires an exceptionally high callose synthesis rate.Significance StatementPlant cell division features the development of a unique membrane network called the cell plate that matures to a cell wall which separates the two daughter cells. During cell plate development, callose, a β-1-3 glucan polymer, is transiently synthesized at the cell plate only to be replaced by cellulose in mature stages. The role for this transient callose accumulation at the cell plate is unknown. It has been suggested that callose provides mechanical stability, as well as a spreading force that widens and expands tubular and fenestrated cell plate structures to aid the maturation of the cell plate. Chemical inhibition of callose deposition results in the failure of cell plate development supporting this hypothesis. This publication establishes the need for a spreading force in cell plate development using a biophysical model that predicts cell plate development in the presence and the absence of this force. Such models can potentially be used to decipher for the transition/maturation of membrane networks upon the deposition of polysaccharide polymers.

scholarly journals LysPBC2, a Novel Endolysin Harboring aBacillus cereusSpore Binding Domain

2018 ◽  
Vol 85 (5) ◽  
Author(s):  
Minsuk Kong ◽  
Hongjun Na ◽  
Nam-Chul Ha ◽  
Sangryeol Ryu
Keyword(s):  
Cell Wall ◽  
Catalytic Domain ◽  
Binding Activity ◽  
Binding Domain ◽  
Lytic Activity ◽  
Content Type ◽  
Cell Wall Binding ◽  
A Cell ◽  
Cell Wall Binding Domain

ABSTRACTTo control the spore-forming human pathogenBacillus cereus, we isolated and characterized a novel endolysin, LysPBC2, from a newly isolatedB. cereusphage, PBC2. Compared to the narrow host range of phage PBC2, LysPBC2 showed very broad lytic activity against allBacillus,Listeria, andClostridiumspecies tested. In addition to a catalytic domain and a cell wall binding domain, LysPBC2 has a spore binding domain (SBD) partially overlapping its catalytic domain, which specifically binds toB. cereusspores but not to vegetative cells ofB. cereus. Both immunogold electron microscopy and a binding assay indicated that the SBD binds the external region of the spore cortex layer. Several amino acid residues required for catalytic or spore binding activity of LysPBC2 were determined by mutagenesis studies. Interestingly, LysPBC2 derivatives with impaired spore binding activity showed an increased lytic activity against vegetative cells ofB. cereuscompared with that of wild-type LysPBC2. Further biochemical studies revealed that these LysPBC2 derivatives have lower thermal stability, suggesting a stabilizing role of SBD in LysPBC2 structure.IMPORTANCEBacteriophages produce highly evolved lytic enzymes, called endolysins, to lyse peptidoglycan and release their progeny from bacterial cells. Due to their potent lytic activity and specificity, the use of endolysins has gained increasing attention as a natural alternative to antibiotics. Since most endolysins from Gram-positive-bacterium-infecting phages have a modular structure, understanding the function of each domain is crucial to make effective endolysin-based therapeutics. Here, we report the functional and biochemical characterization of aBacillus cereusphage endolysin, LysPBC2, which has an unusual spore binding domain and a cell wall binding domain. A single point mutation in the spore binding domain greatly enhanced the lytic activity of endolysin at the cost of reduced thermostability. This work contributes to the understanding of the role of each domain in LysPBC2 and will provide insight for the rational design of efficient antimicrobials or diagnostic tools for controllingB. cereus.

scholarly journals Endopolygalacturonase Is Essential for Citrus Black Rot Caused by Alternaria citri but Not Brown Spot Caused by Alternaria alternata

2001 ◽  
Vol 14 (6) ◽  
pp. 749-757 ◽  
Author(s):  
Atsunori Isshiki ◽  
Kazuya Akimitsu ◽  
Mikihiro Yamamoto ◽  
Hiroyuki Yamamoto
Keyword(s):  
Cell Wall ◽  
Alternaria Alternata ◽  
Biochemical Properties ◽  
Brown Spot ◽  
Black Rot ◽  
Citrus Peel ◽  
Degrading Enzyme ◽  
Cell Wall Degrading Enzyme ◽  
A Cell

Alternaria citri, the cause of Alternaria black rot, and Alternaria alternata rough lemon pathotype, the cause of Alternaria brown spot, are morphologically indistinguishable pathogens of citrus: one causes rot by macerating tissues and the other causes necrotic spots by producing a host-selective toxin. To evaluate the role of endopolygalacturonase (endoPG) in pathogenicity of these two Alternaria spp. pathogens, their genes for endoPG were mutated by gene targeting. The endoPGs produced by these fungi have similar biochemical properties, and the genes are highly similar (99.6% nucleotide identity). The phenotypes of the mutants, however, are completely different. An endoPG mutant of A. citri was significantly reduced in its ability to cause black rot symptoms on citrus as well as in the maceration of potato tissue and could not colonize citrus peel segments. In contrast, an endoPG mutant of A. alternata was unchanged in pathogenicity. The results indicate that a cell wall-degrading enzyme can play different roles in the pathogenicity of fungal pathogens. The role of a cell wall-degrading enzyme depends upon the type of disease but not the taxonomy of the fungus.

scholarly journals Molecular Insights on exquisitely Selective SrtA inhibitors towards active site loop forming open/close lid conformations in SrtA from Bacillus anthracis

2019 ◽  
Author(s):  
Chandrabose Selvaraj ◽  
Gurudeeban Selvaraj ◽  
Satyavani Kaliamurthi ◽  
Dong-Qing Wei ◽  
Sanjeev Kumar Singh
Keyword(s):  
Cell Wall ◽  
Bacillus Anthracis ◽  
Conformational Changes ◽  
Active Site ◽  
3D Qsar ◽  
Sortase A ◽  
Protein Conformational Changes ◽  
A Cell ◽  
Inhibitory Activities

AbstractThe present study clearly explains the dependency of inhibitory activities in SrtA inhibitors is closely related to protein conformational changes of SrtA from Bacillus anthracis B. anthracisSortase A (SrtA) protein anchors proteins by recognizing a cell wall sorting signal containing the amino acid sequence LPXTG In order to analyze conformational changes and the role of SrtA enzyme, especially the loop motions which situated proximal to the active site molecular dynamic simulation was carried out for 100ns. Particular loop is examined for its various conformations from the MD trajectories and the open/close lid conformations are considered for the enzyme activity validations. Experimentally verified SrtA inhibitors activity was analyzed through 3D-QSAR and Molecular docking approaches. Results indicate that, biological activity of SrtA inhibitors is closely related to the closed lid conformation of SrtA from Bacillus anthracis. This work may lead to a better understanding of the mechanism of action and aid to design a novel and more potent SrtA inhibitors.

scholarly journals Role of the Murein Precursor UDP-N-Acetylmuramyl-l-Ala-γ-d-Glu- meso-Diaminopimelic Acid-d-Ala-d-Ala in Repression of β-Lactamase Induction in Cell Division Mutants

2002 ◽  
Vol 184 (15) ◽  
pp. 4233-4239 ◽  
Author(s):  
Tsuyoshi Uehara ◽  
James T. Park
Keyword(s):  
Cell Wall ◽  
Cell Division ◽  
High Ratio ◽  
Diaminopimelic Acid ◽  
Breakdown Product ◽  
A Cell ◽  
Cell Wall Breakdown ◽  
Ts Mutant

ABSTRACT Certain β-lactam antibiotics induce the chromosomal ampC β-lactamase of many gram-negative bacteria. The natural inducer, though not yet unequivocally identified, is a cell wall breakdown product which enters the cell via the AmpG permease component of the murein recycling pathway. Surprisingly, it has been reported that β-lactamase is not induced by cefoxitin in the absence of FtsZ, which is required for cell division, or in the absence of penicillin-binding protein 2 (PBP2), which is required for cell elongation. Since these results remain unexplained, we examined an ftsZ mutant and other cell division mutants (ftsA, ftsQ, and ftsI) and a PBP2 mutant for induction of β-lactamase. In all mutants, β-lactamase was not induced by cefoxitin, which confirms the initial reports. The murein precursor, UDP-N-acetylmuramyl-l-Ala-γ-d-Glu-meso-diaminopimelic acid-d-Ala-d-Ala (UDP-MurNAc-pentapeptide), has been shown to serve as a corepressor with AmpR to repress β-lactamase expression in vitro. Our results suggest that β-lactamase is not induced because the fts mutants contain a greatly increased amount of corepressor which the inducer cannot displace. In the PBP2(Ts) mutant, in addition to accumulation of corepressor, cell wall turnover and recycling were greatly reduced so that little or no inducer was available. Hence, in both cases, a high ratio of repressor to inducer presumably prevents induction.

scholarly journals Role of Hog1 and Yaf9 in the transcriptional response ofSaccharomyces cerevisiaeto cesium chloride

2008 ◽  
Vol 33 (1) ◽  
pp. 110-120 ◽  
Author(s):  
Valerio Del Vescovo ◽  
Viviana Casagrande ◽  
Michele M. Bianchi ◽  
Eugenia Piccinni ◽  
Laura Frontali ◽  
...  
Keyword(s):  
Cell Wall ◽  
Transcriptional Response ◽  
Cesium Chloride ◽  
Wall Structure ◽  
Double Deletion ◽  
Transcriptional Modulation ◽  
A Cell ◽  
Restructuring Process ◽  
Hog1 Phosphorylation

We analyzed the global transcriptional response of Saccharomyces cerevisiae cells exposed to different concentrations of CsCl in the growth medium and at different times after addition. Early responsive genes were mainly involved in cell wall structure and biosynthesis. About half of the induced genes were previously shown to respond to other alkali metal cations in a Hog1-dependent fashion. Western blot analysis confirmed that cesium concentrations as low as 100 mM activate Hog1 phosphorylation. Another important fraction of the cesium-modulated genes requires Yaf9p for full responsiveness as shown by the transcriptome of a yaf9-deleted strain in the presence of cesium. We showed that a cell wall-restructuring process promptly occurs in response to cesium addition, which is dependent on the presence of both Hog1 and Yaf9 proteins. Moreover, the sensitivity to low concentration of cesium of the yaf9-deleted strain is not observed in a strain carrying the hog1/ yaf9 double deletion. We conclude that the observed early transcriptional modulation of cell wall genes has a crucial role in S. cerevisiae adaptation to cesium.

Influence of a Cell-Wall-Associated Protease on Production of α-Amylase by Bacillus subtilis

1998 ◽  
Vol 64 (8) ◽  
pp. 2875-2881 ◽  
Author(s):  
Keith Stephenson ◽  
Colin R. Harwood
Keyword(s):  
Cell Wall ◽  
Bacillus Subtilis ◽  
Bacillus Licheniformis ◽  
Potential Role ◽  
Heterologous Proteins ◽  
Extracellular Proteases ◽  
Serine Protease Activity ◽  
A Cell ◽  
Processed Products

ABSTRACT AmyL, an extracellular α-amylase from Bacillus licheniformis, is resistant to extracellular proteases secreted by Bacillus subtilis during growth. Nevertheless, when AmyL is produced and secreted by B. subtilis, it is subject to considerable cell-associated proteolysis. Cell-wall-bound proteins CWBP52 and CWBP23 are the processed products of the B. subtilis wprA gene. Although no activity has been ascribed to CWBP23, CWBP52 exhibits serine protease activity. Using a strain encoding an inducible wprA gene, we show that a product of wprA, most likely CWBP52, is involved in the posttranslocational stability of AmyL. A construct in whichwprA is not expressed exhibits an increased yield of α-amylase. The potential role of wprA in protein secretion is discussed, together with implications for the use ofB. subtilis and related bacteria as hosts for the secretion of heterologous proteins.

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