scholarly journals Updating Insights into the Catalytic Domain Properties of Plant Cellulose synthase (CesA) and Cellulose synthase-like (Csl) Proteins

Molecules ◽  
2021 ◽  
Vol 26 (14) ◽  
pp. 4335
Author(s):  
Gerasimos Daras ◽  
Dimitris Templalexis ◽  
Fengoula Avgeri ◽  
Dikran Tsitsekian ◽  
Konstantina Karamanou ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Economic Value ◽  
Cellulose Synthase ◽  
Protein Isoforms ◽  
Research Progress ◽  
Cellulose Synthesis ◽  
Biotic Stresses

The wall is the last frontier of a plant cell involved in modulating growth, development and defense against biotic stresses. Cellulose and additional polysaccharides of plant cell walls are the most abundant biopolymers on earth, having increased in economic value and thereby attracted significant interest in biotechnology. Cellulose biosynthesis constitutes a highly complicated process relying on the formation of cellulose synthase complexes. Cellulose synthase (CesA) and Cellulose synthase-like (Csl) genes encode enzymes that synthesize cellulose and most hemicellulosic polysaccharides. Arabidopsis and rice are invaluable genetic models and reliable representatives of land plants to comprehend cell wall synthesis. During the past two decades, enormous research progress has been made to understand the mechanisms of cellulose synthesis and construction of the plant cell wall. A plethora of cesa and csl mutants have been characterized, providing functional insights into individual protein isoforms. Recent structural studies have uncovered the mode of CesA assembly and the dynamics of cellulose production. Genetics and structural biology have generated new knowledge and have accelerated the pace of discovery in this field, ultimately opening perspectives towards cellulose synthesis manipulation. This review provides an overview of the major breakthroughs gathering previous and recent genetic and structural advancements, focusing on the function of CesA and Csl catalytic domain in plants.

scholarly journals Dependence of Plant Cell Wall Composition and Structure on Cellulose Synthase-Like Knock Out Mutant

2012 ◽  
Vol 102 (3) ◽  
pp. 590a-591a
Author(s):  
Andreia M. Smith-Moritz ◽  
Jeemeng Lao ◽  
Joshua L. Heazlewood ◽  
Pamela C. Ronald ◽  
Miguel E. Vega-Sanchez
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Cellulose Synthase ◽  
Cell Wall Composition ◽  
Knock Out ◽  
Composition And Structure

scholarly journals Identification of Putative Cell Wall Synthesis Genes in Betula pendula

2020 ◽  
Author(s):  
Song Chen ◽  
Xin Lin ◽  
Xiyang Zhao ◽  
Su Chen
Keyword(s):  
Cell Wall ◽  
Betula Pendula ◽  
Secondary Cell Wall ◽  
Plant Cell Wall ◽  
Gene Families ◽  
Cellulose Synthase ◽  
Wall Structure ◽  
Cellulose Synthesis ◽  
Cell Wall Synthesis ◽  
Secondary Cell Wall Synthesis

Abstract BackgroundCellulose is an essential structural component of plant cell wall and is an important resource to produce paper, textiles, bioplastics and other biomaterials. The synthesis of cellulose is among the most important but poorly understood biochemical processes, which is precisely regulated by internal and external cues.ResultsHere, we identified 46 gene models in 7 gene families which encoding cellulose synthase and related enzymes of Betula pendula, and the transcript abundance of these genes in xylem, root, leaf and flower tissues also be determined. Based on these RNA-seq data, we have identified 8 genes that most likely participate in secondary cell wall synthesis, which include 3 cellulose synthase genes and 5 cellulose synthase-like genes. In parallel, a gene co-expression network was also constructed based on transcriptome sequencing.ConclusionsIn this study, we have identified a total of 46 cell wall synthesis genes in B. pendula, which include 8 secondary cell wall synthesis genes. These analyses will help decipher the genetic information of the cell wall synthesis genes, elucidate the molecular mechanism of cellulose synthesis and understand the cell wall structure in B. pendula.

scholarly journals Crystallization and preliminary crystallographic studies of a novel noncatalytic carbohydrate-binding module from theRuminococcus flavefacienscellulosome

2015 ◽  
Vol 71 (1) ◽  
pp. 45-48 ◽  
Author(s):  
Immacolata Venditto ◽  
Arun Goyal ◽  
Andrew Thompson ◽  
Luis M. A. Ferreira ◽  
Carlos M. G. A. Fontes ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Cellulolytic Bacterium ◽  
Modular Architecture ◽  
Carbohydrate Binding Modules ◽  
Fundamental Biological Process

Microbial degradation of the plant cell wall is a fundamental biological process with considerable industrial importance. Hydrolysis of recalcitrant polysaccharides is orchestrated by a large repertoire of carbohydrate-active enzymes that display a modular architecture in which a catalytic domain is connectedvialinker sequences to one or more noncatalytic carbohydrate-binding modules (CBMs). CBMs direct the appended catalytic modules to their target substrates, thus potentiating catalysis. The genome of the most abundant ruminal cellulolytic bacterium,Ruminococcus flavefaciensstrain FD-1, provides an opportunity to discover novel cellulosomal proteins involved in plant cell-wall deconstruction. It encodes a modular protein comprising a glycoside hydrolase family 9 catalytic module (GH9) linked to two unclassified tandemly repeated CBMs (termed CBM-Rf6A and CBM-Rf6B) and a C-terminal dockerin. The novel CBM-Rf6A from this protein has been crystallized and data were processed for the native and a selenomethionine derivative to 1.75 and 1.5 Å resolution, respectively. The crystals belonged to orthorhombic and cubic space groups, respectively. The structure was solved by a single-wavelength anomalous dispersion experiment using theCCP4 program suite andSHELXC/D/E.

scholarly journals Plant Cell Wall as a Key Player During Resistant and Susceptible Plant-Virus Interactions

2021 ◽  
Vol 12 ◽  
Author(s):  
Edmund Kozieł ◽  
Katarzyna Otulak-Kozieł ◽  
Józef Julian Bujarski
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Virus ◽  
Defense Mechanisms ◽  
Fungal Pathogens ◽  
Plant Cell Wall ◽  
Viral Infections ◽  
Structural Element ◽  
Biotic Stresses ◽  
New Research

The cell wall is a complex and integral part of the plant cell. As a structural element it sustains the shape of the cell and mediates contact among internal and external factors. We have been aware of its involvement in both abiotic (like drought or frost) and biotic stresses (like bacteria or fungi) for some time. In contrast to bacterial and fungal pathogens, viruses are not mechanical destructors of host cell walls, but relatively little is known about remodeling of the plant cell wall in response to viral biotic stress. New research results indicate that the cell wall represents a crucial active component during the plant’s response to different viral infections. Apparently, cell wall genes and proteins play key roles during interaction, having a direct influence on the rebuilding of the cell wall architecture. The plant cell wall is involved in both susceptibility as well as resistance reactions. In this review we summarize important progress made in research on plant virus impact on cell wall remodeling. Analyses of essential defensive wall associated proteins in susceptible and resistant responses demonstrate that the components of cell wall metabolism can affect the spread of the virus as well as activate the apoplast- and symplast-based defense mechanisms, thus contributing to the complex network of the plant immune system. Although the cell wall reorganization during the plant-virus interaction remains a challenging task, the use of novel tools and methods to investigate its composition and structure will greatly contribute to our knowledge in the field.

scholarly journals A non-modular endo-β-1,4-mannanase from Pseudomonas fluorescens subspecies cellulosa

1995 ◽  
Vol 305 (3) ◽  
pp. 1005-1010 ◽  
Author(s):  
K L Braithwaite ◽  
G W Black ◽  
G P Hazlewood ◽  
B R S Ali ◽  
H J Gilbert
Keyword(s):  
Cell Wall ◽  
Pseudomonas Fluorescens ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Genomic Library ◽  
Glycosyl Hydrolase ◽  
Ph Optimum ◽  
Reading Frame ◽  
Protein Motifs

Pseudomonas fluorescens subsp. cellulosa when cultured in the presence of carob galactomannan degraded the polysaccharide. To isolate gene(s) from P. fluorescens subsp. cellulosa encoding endo-beta-1,4-mannanase (mannanase) activity, a genomic library of Pseudomonas DNA, constructed in lambda ZAPII, was screened for mannanase-expressing clones using the dye-labelled substrate, azo-carob galactomannan. The nucleotide sequence of the pseudomonad insert from a mannanase-positive clone revealed a single open reading frame of 1257 bp encoding a protein of M(r) 46,938. The deduced N-terminal sequence of the putative polypeptide conformed to a typical prokaryotic signal peptide. Truncated derivatives of the mannanase, lacking 54 and 16 residues from the N- and C-terminus respectively of the mature form of the enzyme, did not exhibit catalytic activity. Inspection of the primary structure of the mannanase did not reveal any obvious linker sequences or protein motifs characteristic of the non-catalytic domains located in other Pseudomonas plant cell wall hydrolases. These data indicate that the mannanase is non-modulator, comprising a single catalytic domain. Comparison of the mannanase sequence with those in the SWISSPROT database revealed greatest sequence homology with the mannanase from Bacillus sp. Thus the Pseudomonas enzyme belongs to glycosyl hydrolase Family 26, a family containing mannanases and endoglucanases. Analysis of the substrate specificity of the mannanase showed that the enzyme hydrolysed mannan and galactomannan, but displayed little activity towards other polysaccharides located in the plant cell wall. The enzyme had a pH optimum of approx. 7.0, was resistant to proteolysis and had an M(r) of 46,000 when expressed by Escherichia coli.

scholarly journals Architecture of a catalytically active homotrimeric plant cellulose synthase complex

Science ◽  
2020 ◽  
Vol 369 (6507) ◽  
pp. 1089-1094 ◽  
Author(s):  
Pallinti Purushotham ◽  
Ruoya Ho ◽  
Jochen Zimmer
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Molecular Basis ◽  
Plant Cell Wall ◽  
Cellulose Synthase ◽  
Exit Point ◽  
Transmembrane Segments ◽  
Catalytically Active ◽  
Cellulose Synthase Complex ◽  
Microfibril Formation

Cellulose is an essential plant cell wall component and represents the most abundant biopolymer on Earth. Supramolecular plant cellulose synthase complexes organize multiple linear glucose polymers into microfibrils as load-bearing wall components. We determined the structure of a poplar cellulose synthase CesA homotrimer that suggests a molecular basis for cellulose microfibril formation. This complex, stabilized by cytosolic plant-conserved regions and helical exchange within the transmembrane segments, forms three channels occupied by nascent cellulose polymers. Secretion steers the polymers toward a common exit point, which could facilitate protofibril formation. CesA’s N-terminal domains assemble into a cytosolic stalk that interacts with a microtubule-tethering protein and may thus be involved in CesA localization. Our data suggest how cellulose synthase complexes assemble and provide the molecular basis for plant cell wall engineering.

Genetic dissection of plant cell-wall biosynthesis

2002 ◽  
Vol 30 (2) ◽  
pp. 298-301 ◽  
Author(s):  
D. T. Bonetta ◽  
M. Facette ◽  
T. K. Raab ◽  
C. R. Somerville
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Mutant Cell ◽  
Complex Structure ◽  
Exchange Chromatography ◽  
Phenotypic Characterization ◽  
Composition Analysis ◽  
Cellulose Synthesis ◽  
Neutral Sugar

The plant cell wall is a complex structure consisting of a variety of polymers including cellulose, xyloglucan, xylan and polygalacturonan. Biochemical and genetic analysis has made it possible to clone genes encoding cellulose synthases (CesA). A comparison of the predicted protein sequences in the Arabidopsis genome indicates that 30 divergent genes with similarity to CesAs exist. It is possible that these cellulose synthase-like (Csl) proteins do not contribute to cellulose synthesis, but rather to the synthesis of other wall polymers. A major challenge is, therefore, to assign biological function to these genes. In an effort to address this issue we have systematically identified T-DNA or transposon insertions in 17 Arabidopsis Csls. Phenotypic characterization of ‘knock-out’ mutants includes the determination of spectroscopic profile differences in mutant cell walls from wild-type plants by Fourier-transform IR microscopy. A more precise characterization includes cell wall fractionation followed by neutral sugar composition analysis by anionic exchange chromatography.

scholarly journals Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria

1995 ◽  
Vol 307 (1) ◽  
pp. 151-158 ◽  
Author(s):  
C M G A Fontes ◽  
G P Hazlewood ◽  
E Morag ◽  
J Hall ◽  
B H Hirst ◽  
...  
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Genomic Library ◽  
Thermophilic Bacteria ◽  
Cross Hybridization ◽  
General Role ◽  
Sequence Identity ◽  
Cell Wall Hydrolases

A genomic library of Clostridium thermocellum DNA constructed in lambda ZAPII was screened for xylanase-expressing clones. Cross-hybridization experiments revealed a new xylanase gene isolated from the gene library, which was designated xyn Y. The encoded enzyme, xylanase Y (XYLY), displayed features characteristic of an endo-beta1,4-xylanase: the enzyme rapidly hydrolysed oat spelt, wheat and rye arabinoxylans and was active against methyl-umbelliferyl-beta-D-cellobioside, but did not hydrolyse any cellulosic substrates. The pH and temperature optima of the enzyme were 6.8 and 75 degrees C respectively, and the recombinant XYLY, expressed by Escherichia coli had a maximum Mr of 116000. The nucleotide sequence of xyn Y contained an open reading frame of 3228 bp encoding a protein of predicted Mr 120 105. The encoded enzyme contained a typical N-terminal 26-residue signal peptide, followed by a 164 amino acid sequence, designated domain A, that was not essential for catalytic activity. Downstream of domain A was a 351-residue xylanase Family F catalytic domain, followed by a 180-residue sequence that exhibited 28% sequence identity with a thermostable domain of Thermoanaerobacterium saccharolyticum xylanase A. The C-terminal portion of XYLY comprised the 23-residue duplicated docking sequence found in all other C. thermocellum plant cell wall hydrolases that are constituents of the bacterium's multienzyme complex, termed the cellulosome, followed by a 286-residue domain which exhibited 32% sequence identity with the N-terminal region of C. thermocellum xylanase Z. The enzyme did not contain linker sequences found in other C. thermocellum plant cell wall hydrolases. Analysis of truncated forms of XYLY and hybrid proteins, comprising segments of XYLY fused to the E. coli maltose binding domain, confirmed that XYLY contained a central catalytic domain and an adjacent thermostable domain. The C-terminal domain did not bind to cellulose or xylan. Western blot analysis using antiserum raised against XYLY showed that the xylanase was located in the cellulosome and did not appear to be extensively glycosylated. The non-catalytic domains of XYLY are discussed in relation to the general stability of thermophilic xylanases.

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