scholarly journals Promotion of Efficient Saccharification of Crystalline Cellulose by Aspergillus fumigatus Swo1

2010 ◽  
Vol 76 (8) ◽  
pp. 2556-2561 ◽  
Author(s):  
Xin-ai Chen ◽  
Nobuhiro Ishida ◽  
Nemuri Todaka ◽  
Risa Nakamura ◽  
Jun-ichi Maruyama ◽  
...  
Keyword(s):  
Cell Wall ◽  
Aspergillus Fumigatus ◽  
Plant Cell Wall ◽  
Sequence Similarity ◽  
Crystalline Cellulose ◽  
Carbohydrate Binding ◽  
Cell Wall Proteins ◽  
Gene Encoding ◽  
Endoglucanase Activity ◽  
Novel Approach

ABSTRACT Swollenin is a protein from Trichoderma reesei that has a unique activity for disrupting cellulosic materials, and it has sequence similarity to expansins, plant cell wall proteins that have a loosening effect that leads to cell wall enlargement. In this study we cloned a gene encoding a swollenin-like protein, Swo1, from the filamentous fungus Aspergillus fumigatus, and designated the gene Afswo1. AfSwo1 has a bimodular structure composed of a carbohydrate-binding module family 1 (CBM1) domain and a plant expansin-like domain. AfSwo1 was produced using Aspergillus oryzae for heterologous expression and was easily isolated by cellulose-affinity chromatography. AfSwo1 exhibited weak endoglucanase activity toward carboxymethyl cellulose (CMC) and bound not only to crystalline cellulose Avicel but also to chitin, while showing no detectable affinity to xylan. Treatment by AfSwo1 caused disruption of Avicel into smaller particles without any detectable reducing sugar. Furthermore, simultaneous incubation of AfSwo1 with a cellulase mixture facilitated saccharification of Avicel. Our results provide a novel approach for efficient bioconversion of crystalline cellulose into glucose by use of the cellulose-disrupting protein AfSwo1.

scholarly journals Slipped strand mispairing in the gene encoding sialidase NanH3 in Gardnerella spp

2020 ◽  
Author(s):  
Shakya P. Kurukulasuriya ◽  
Mo H. Patterson ◽  
Janet E. Hill
Keyword(s):  
Cell Wall ◽  
Biofilm Formation ◽  
Gene Sequence ◽  
Phase Variation ◽  
Cell Wall Proteins ◽  
Vaginal Microbiome ◽  
Gene Encoding ◽  
Reading Frame ◽  
Sialidase Activity ◽  
Mucosal Surfaces

AbstractCell wall proteins with sialidase activity are involved in carbohydrate assimilation, adhesion to mucosal surfaces, and biofilm formation. Gardnerella spp. inhabit the human vaginal microbiome and encode up to three sialidase enzymes, two of which are suspected to be cell wall associated. Here we demonstrate that the gene encoding extracellular sialidase NanH3 is found almost exclusively in G. piotii and closely related Gardnerella genome sp. 3, and its presence correlates with sialidase positive phenotype in a collection of 112 Gardnerella isolates. The nanH3 gene sequence includes a homopolymeric repeat of cytosines that varies in length within cell populations, indicating that this gene is subject to slipped-strand mispairing, a mechanisms of phase variation in bacteria. Variation in the length of the homopolymer sequence results in encoding of either the full length sialidase protein or truncated peptides lacking the sialidase domain due to introduction of reading-frame shifts and premature stop codons. Phase variation in NanH3 may be involved in immune evasion or modulation of adhesion to host epithelial cells, and formation of biofilms characteristic of the vaginal dysbiosis known as bacterial vaginosis.

scholarly journals Cellulose synthase interactive1- and microtubule-dependent cell wall architecture is required for acid growth in Arabidopsis hypocotyls

2020 ◽  
Vol 71 (10) ◽  
pp. 2982-2994 ◽  
Author(s):  
Xiaoran Xin ◽  
Lei Lei ◽  
Yunzhen Zheng ◽  
Tian Zhang ◽  
Sai Venkatesh Pingali ◽  
...  
Keyword(s):  
Cell Wall ◽  
Cell Elongation ◽  
Plant Cell Wall ◽  
Cellulose Microfibrils ◽  
Crystalline Cellulose ◽  
Cellulose Content ◽  
Acid Growth ◽  
Cell Wall Assembly ◽  
Dependent Cell ◽  
Cell Wall Architecture

Abstract Auxin-induced cell elongation relies in part on the acidification of the cell wall, a process known as acid growth that presumably triggers expansin-mediated wall loosening via altered interactions between cellulose microfibrils. Cellulose microfibrils are a major determinant for anisotropic growth and they provide the scaffold for cell wall assembly. Little is known about how acid growth depends on cell wall architecture. To explore the relationship between acid growth-mediated cell elongation and plant cell wall architecture, two mutants (jia1-1 and csi1-3) that are defective in cellulose biosynthesis and cellulose microfibril organization were analyzed. The study revealed that cell elongation is dependent on CSI1-mediated cell wall architecture but not on the overall crystalline cellulose content. We observed a correlation between loss of crossed-polylamellate walls and loss of auxin- and fusicoccin-induced cell growth in csi1-3. Furthermore, induced loss of crossed-polylamellate walls via disruption of cortical microtubules mimics the effect of csi1 in acid growth. We hypothesize that CSI1- and microtubule-dependent crossed-polylamellate walls are required for acid growth in Arabidopsis hypocotyls.

Analysis of the Structural and Functional Diversity of Plant Cell Wall Specific Family 6 Carbohydrate Binding Modules

Biochemistry ◽  
2009 ◽  
Vol 48 (43) ◽  
pp. 10395-10404 ◽  
Author(s):  
D. Wade Abbott ◽  
Elizabeth Ficko-Blean ◽  
Alicia Lammerts van Bueren ◽  
Artur Rogowski ◽  
Alan Cartmell ◽  
...  
Keyword(s):  
Cell Wall ◽  
Functional Diversity ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules

Plant Cell Wall Proteins and Auxin-Induced Growth

1991 ◽  
Vol 137 (6) ◽  
pp. 765-767 ◽  
Author(s):  
Bernhard Gugsch ◽  
Dieter Klämbt
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Cell Wall Proteins

scholarly journals The modular architecture of Cellvibrio japonicus mannanases in glycoside hydrolase families 5 and 26 points to differences in their role in mannan degradation

2003 ◽  
Vol 371 (3) ◽  
pp. 1027-1043 ◽  
Author(s):  
Deborah HOGG ◽  
Gavin PELL ◽  
Paul DUPREE ◽  
Florence GOUBET ◽  
Susana M. MARTÍN-ORÚE ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Catalytic Domain ◽  
Glycoside Hydrolases ◽  
Crystalline Cellulose ◽  
Carbohydrate Binding ◽  
Molecular Architecture ◽  
Catalytic Domains ◽  
Carbohydrate Binding Modules ◽  
Cellvibrio Japonicus

β-1,4-Mannanases (mannanases), which hydrolyse mannans and glucomannans, are located in glycoside hydrolase families (GHs) 5 and 26. To investigate whether there are fundamental differences in the molecular architecture and biochemical properties of GH5 and GH26 mannanases, four genes encoding these enzymes were isolated from Cellvibrio japonicus and the encoded glycoside hydrolases were characterized. The four genes, man5A, man5B, man5C and man26B, encode the mannanases Man5A, Man5B, Man5C and Man26B, respectively. Man26B consists of an N-terminal signal peptide linked via an extended serine-rich region to a GH26 catalytic domain. Man5A, Man5B and Man5C contain GH5 catalytic domains and non-catalytic carbohydrate-binding modules (CBMs) belonging to families 2a, 5 and 10; Man5C in addition contains a module defined as X4 of unknown function. The family 10 and 2a CBMs bound to crystalline cellulose and ivory nut crystalline mannan, displaying very similar properties to the corresponding family 10 and 2a CBMs from Cellvibrio cellulases and xylanases. CBM5 bound weakly to these crystalline polysaccharides. The catalytic domains of Man5A, Man5B and Man26B hydrolysed galactomannan and glucomannan, but displayed no activity against crystalline mannan or cellulosic substrates. Although Man5C was less active against glucomannan and galactomannan than the other mannanases, it did attack crystalline ivory nut mannan. All the enzymes exhibited classic endo-activity producing a mixture of oligosaccharides during the initial phase of the reaction, although their mode of action against manno-oligosaccharides and glucomannan indicated differences in the topology of the respective substrate-binding sites. This report points to a different role for GH5 and GH26 mannanases from C. japonicus. We propose that as the GH5 enzymes contain CBMs that bind crystalline polysaccharides, these enzymes are likely to target mannans that are integral to the plant cell wall, while GH26 mannanases, which lack CBMs and rapidly release mannose from polysaccharides and oligosaccharides, target the storage polysaccharide galactomannan and manno-oligosaccharides.

Glycoside hydrolase carbohydrate-binding modules as molecular probes for the analysis of plant cell wall polymers

2004 ◽  
Vol 326 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Lesley McCartney ◽  
Harry J Gilbert ◽  
David N Bolam ◽  
Alisdair B Boraston ◽  
J.Paul Knox
Keyword(s):  
Cell Wall ◽  
Plant Cell ◽  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Molecular Probes ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules ◽  
Cell Wall Polymers

scholarly journals Investigation of cell wall proteins of C. sinensis leaves by combining cell wall proteomics and N-glycoproteomics

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Yanli Liu ◽  
Linlong Ma ◽  
Dan Cao ◽  
Ziming Gong ◽  
Jing Fan ◽  
...  
Keyword(s):  
Cell Wall ◽  
Defense Response ◽  
Large Scale ◽  
Plant Cell Wall ◽  
Functional Class ◽  
Wall Structure ◽  
Cell Wall Proteins ◽  
Cell Wall Formation ◽  
Cell Wall Polysaccharides ◽  
Wall Formation

Abstract Background C. sinensis is an important economic crop with fluoride over-accumulation in its leaves, which poses a serious threat to human health due to its leaf consumption as tea. Recently, our study has indicated that cell wall proteins (CWPs) probably play a vital role in fluoride accumulation/detoxification in C. sinensis. However, there has been a lack in CWP identification and characterization up to now. This study is aimed to characterize cell wall proteome of C. sinensis leaves and to develop more CWPs related to stress response. A strategy of combined cell wall proteomics and N-glycoproteomics was employed to investigate CWPs. CWPs were extracted by sequential salt buffers, while N-glycoproteins were enriched by hydrophilic interaction chromatography method using C. sinensis leaves as a material. Afterwards all the proteins were subjected to UPLC-MS/MS analysis. Results A total of 501 CWPs and 195 CWPs were identified respectively by cell wall proteomics and N-glycoproteomics profiling with 118 CWPs in common. Notably, N-glycoproteomics is a feasible method for CWP identification, and it can enhance CWP coverage. Among identified CWPs, proteins acting on cell wall polysaccharides constitute the largest functional class, most of which might be involved in cell wall structure remodeling. The second largest functional class mainly encompass various proteases related to CWP turnover and maturation. Oxidoreductases represent the third largest functional class, most of which (especially Class III peroxidases) participate in defense response. As expected, identified CWPs are mainly related to plant cell wall formation and defense response. Conclusion This was the first large-scale investigation of CWPs in C. sinensis through cell wall proteomics and N-glycoproteomics. Our results not only provide a database for further research on CWPs, but also an insight into cell wall formation and defense response in C. sinensis.

scholarly journals Defensive forwards: stress-responsive proteins in cell walls of crop plants

2020 ◽  
Author(s):  
Liangjie Niu ◽  
Wei Wang
Keyword(s):  
Cell Wall ◽  
Stress Responses ◽  
Plant Cell Wall ◽  
Strong Interactions ◽  
Wall Structure ◽  
Cell Wall Proteins ◽  
Go Annotation ◽  
Gene Differential Expression ◽  
Expression Atlas ◽  
Specific Proteins

ABSTRACTAs the vital component of plant cell wall, proteins play important roles in stress response through modifying wall structure and involving in wall integrity signaling. However, the potential of cell wall proteins (CWPs) in improvement of crop stress tolerance has probably been underestimated. Recently, we have critically reviewed the predictors, databases and cross-referencing of subcellular locations of possible CWPs in plants (Briefings in Bioinformatics 2018;19:1130-1140). In this study, taking maize (Zea mays) as an example, we retrieved 1873 entries of probable maize CWPs recorded in UniProtKB. As a result, 863 maize CWPs are curated and classified as 59 kinds of protein families. By referring to GO annotation and gene differential expression in Expression Atlas, we highlight the potential of CWPs as defensive forwards in abiotic and biotic stress responses. In particular, several CWPs are found to play key roles in adaptation to many stresses. String analysis also reveals possibly strong interactions among many CWPs, especially those stress-responsive enzymes. The results allow us to narrow down the list of CWPs to a few specific proteins that could be candidates to enhance maize resistance.

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