scholarly journals Pectin digestion in herbivorous beetles: Impact of pseudoenzymes exceeds that of their active counterparts

2018 ◽  
Author(s):  
Roy Kirsch ◽  
Grit Kunert ◽  
Heiko Vogel ◽  
Yannick Pauchet
Keyword(s):  
Plant Cell Wall ◽  
Functional Characterization ◽  
Gene Families ◽  
Glycoside Hydrolase Family ◽  
Cell Wall Degrading Enzymes ◽  
Catalytic Function ◽  
Catalytically Active ◽  
Alternative Function ◽  
The Impact ◽  
Hydrolase Family

AbstractMany protein families harbor pseudoenzymes that have lost the catalytic function of their enzymatically active counterparts. Assigning alternative function and importance to these proteins is challenging [1]. Because the evolution towards pseudoenzymes is driven by gene duplication, they often accumulate in multigene families. Plant cell wall-degrading enzymes (PCWDEs) are prominent examples of expanded gene families. The pectolytic glycoside hydrolase family 28 (GH28) allows herbivorous insects to break down the PCW polysaccharide pectin. GH28 in the Phytophaga clade of beetles contains many active enzymes but also many inactive counterparts. Using functional characterization, gene silencing, global transcriptome analyses and recordings of life history traits, we found that not only catalytically active but also inactive GH28 proteins are part of the same pectin-digesting pathway. The robustness and plasticity of this pathway and thus its importance for the beetle is supported by extremely high steady-state expression levels and counter-regulatory mechanisms. Unexpectedly, the impact of pseudoenzymes on the pectin-digesting pathway in Phytophaga beetles exceeds even the influence of their active counterparts, such as a lowered efficiency of food-to-energy conversion and a prolongation of the developmental period.

scholarly journals Biochemical and Functional Characterization of Glycoside Hydrolase Family 16 Genes in Aedes aegypti Larvae: Identification of the Major Digestive β-1,3-Glucanase

2019 ◽  
Vol 10 ◽  
Author(s):  
Raquel Santos Souza ◽  
Maiara do Valle Faria Gama ◽  
Renata Schama ◽  
José Bento Pereira Lima ◽  
Hector Manuel Diaz-Albiter ◽  
...  
Keyword(s):  
Aedes Aegypti ◽  
Glycoside Hydrolase ◽  
Functional Characterization ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals A Metabolic Regulator Modulates Virulence and Quorum Sensing Signal Production in Pectobacterium atrosepticum

2013 ◽  
Vol 26 (3) ◽  
pp. 356-366 ◽  
Author(s):  
Marion F. Cubitt ◽  
Peter E. Hedley ◽  
Neil R. Williamson ◽  
Jenny A. Morris ◽  
Emma Campbell ◽  
...  
Keyword(s):  
Quorum Sensing ◽  
Plant Cell Wall ◽  
Homoserine Lactone ◽  
Insertion Mutation ◽  
Virulence Determinants ◽  
Methionine Biosynthesis ◽  
Cell Wall Degrading Enzymes ◽  
Pectobacterium Atrosepticum ◽  
Small Regulatory Rna ◽  
The Impact

Plant cell wall–degrading enzymes (PCWDE) are key virulence determinants in the pathogenesis of the potato pathogen Pectobacterium atrosepticum. In this study, we report the impact on virulence of a transposon insertion mutation in the metJ gene that codes for the repressor of the methionine biosynthesis regulon. In a mutant strain defective for the small regulatory RNA rsmB, PCWDE are not produced and virulence in potato tubers is almost totally abolished. However, when the metJ gene is disrupted in this background, the rsmB– phenotype is suppressed and virulence and PCWDE production are restored. Additionally, when metJ is disrupted, production of the quorum-sensing signal, N-(3-oxohexanoyl)-homoserine lactone, is increased. The metJ mutant strains showed pleiotropic transcriptional impacts affecting approximately a quarter of the genome. Genes involved in methionine biosynthesis were most highly upregulated but many virulence-associated transcripts were also upregulated. This is the first report of the impact of the MetJ repressor on virulence in bacteria.

scholarly journals Genome-Wide Identification, Expression Pattern Analysis and Evolution of the Ces/Csl Gene Superfamily in Pineapple (Ananas comosus)

Plants ◽  
2019 ◽  
Vol 8 (8) ◽  
pp. 275 ◽  
Author(s):  
Cao ◽  
Cheng ◽  
Zhang ◽  
Aslam ◽  
Yan ◽  
...  
Keyword(s):  
Plant Cell Wall ◽  
Developmental Stages ◽  
Functional Characterization ◽  
Gene Families ◽  
Cellulose Synthase ◽  
Ananas Comosus ◽  
Tropical Fruit ◽  
Genome Wide ◽  
Gene Structures

The cellulose synthase (Ces) and cellulose synthase-like (Csl) gene families belonging to the cellulose synthase gene superfamily, are responsible for the biosynthesis of cellulose and hemicellulose of the plant cell wall, and play critical roles in plant development, growth and evolution. However, the Ces/Csl gene family remains to be characterized in pineapple, a highly valued and delicious tropical fruit. Here, we carried out genome-wide study and identified a total of seven Ces genes and 25 Csl genes in pineapple. Genomic features and phylogeny analysis of Ces/Csl genes were carried out, including phylogenetic tree, chromosomal locations, gene structures, and conserved motifs identification. In addition, we identified 32 pineapple AcoCes/Csl genes with 31 Arabidopsis AtCes/Csl genes as orthologs by the syntenic and phylogenetic approaches. Furthermore, a RNA-seq investigation exhibited the expression profile of several AcoCes/Csl genes in various tissues and multiple developmental stages. Collectively, we provided comprehensive information of the evolution and function of pineapple Ces/Csl gene superfamily, which would be useful for screening out and characterization of the putative genes responsible for tissue development in pineapple. The present study laid the foundation for future functional characterization of Ces/Csl genes in pineapple.

scholarly journals The genome of the mustard leaf beetle encodes two active xylanases originally acquired from bacteria through horizontal gene transfer

2013 ◽  
Vol 280 (1763) ◽  
pp. 20131021 ◽  
Author(s):  
Yannick Pauchet ◽  
David G. Heckel
Keyword(s):  
Cell Wall ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Plant Cell ◽  
Plant Cell Wall ◽  
Genetic Material ◽  
Leaf Beetle ◽  
Glycoside Hydrolase Family ◽  
Cell Wall Degrading Enzymes ◽  
Genes Encoding

The primary plant cell wall comprises the most abundant polysaccharides on the Earth and represents a rich source of energy for organisms which have evolved the ability to digest them. Enzymes able to degrade plant cell wall polysaccharides are widely distributed in micro-organisms but are generally absent in animals, although their presence in insects, especially phytophagous beetles from the superfamilies Chrysomeloidea and Curculionoidea, has recently begun to be appreciated. The observed patchy distribution of endogenous genes encoding these enzymes in animals has raised questions about their evolutionary origins. Recent evidence suggests that endogenous plant cell wall degrading enzymes-encoding genes have been acquired by animals through a mechanism known as horizontal gene transfer (HGT). HGT describes how genetic material is moved by means other than vertical inheritance from a parent to an offspring. Here, we provide evidence that the mustard leaf beetle, Phaedon cochleariae , possesses in its genome genes encoding active xylanases from the glycoside hydrolase family 11 (GH11). We also provide evidence that these genes were originally acquired by P. cochleariae from a species of gammaproteobacteria through HGT. This represents the first example of the presence of genes from the GH11 family in animals.

scholarly journals Protein trafficking in Plasmodium falciparum-infected red cells and impact of the expansion of exported protein families

Parasitology ◽  
2014 ◽  
Vol 141 (12) ◽  
pp. 1533-1543 ◽  
Author(s):  
SURENDRA K. PRAJAPATI ◽  
RICHARD CULLETON ◽  
OM P. SINGH
Keyword(s):  
Plasmodium Falciparum ◽  
Host Cell ◽  
Protein Trafficking ◽  
Malaria Parasite ◽  
Functional Characterization ◽  
Gene Families ◽  
Red Cells ◽  
Protein Families ◽  
The Impact ◽  
Export Signal

SUMMARYErythrocytes are extensively remodelled by the malaria parasite following invasion of the cell. Plasmodium falciparum encodes numerous virulence-associated and host-cell remodelling proteins that are trafficked to the cytoplasm, the cell membrane and the surface of the infected erythrocyte. The export of soluble proteins relies on a sequence directing entry into the secretory pathways in addition to an export signal. The export signal consisting of five amino acids is termed the Plasmodium export element (PEXEL) or the vacuole transport signal (VTS). Genome mining studies have revealed that PEXEL/VTS carrying protein families have expanded dramatically in P. falciparum compared with other malaria parasite species, possibly due to lineage-specific expansion linked to the unique requirements of P. falciparum for host-cell remodelling. The functional characterization of such genes and gene families may reveal potential drug targets that could inhibit protein trafficking in infected erythrocytes. This review highlights some of the recent advances and key knowledge gaps in protein trafficking pathways in P. falciparum-infected red cells and speculates on the impact of exported gene families in the trafficking pathway.

scholarly journals Oligosaccharide Metabolism and Lipoteichoic Acid Production in Lactobacillus gasseri and Lactobacillus paragasseri

2021 ◽  
Vol 9 (8) ◽  
pp. 1590
Author(s):  
Tsukasa Shiraishi ◽  
Shintaro Maeno ◽  
Sayoko Kishi ◽  
Tadashi Fujii ◽  
Hiroki Tanno ◽  
...  
Keyword(s):  
Molecular Size ◽  
Lipoteichoic Acid ◽  
Glycoside Hydrolase Family ◽  
Probiotic Properties ◽  
Lactobacillus Gasseri ◽  
Metabolic Systems ◽  
Metabolic Properties ◽  
The Impact ◽  
Hydrolase Family ◽  
Cells Cultured

Lactobacillus gasseri and Lactobacillus paragasseri are human commensal lactobacilli that are candidates for probiotic application. Knowledge of their oligosaccharide metabolic properties is valuable for synbiotic application. The present study characterized oligosaccharide metabolic systems and their impact on lipoteichoic acid (LTA) production in the two organisms, i.e., L. gasseri JCM 1131T and L. paragasseri JCM 11657. The two strains grew well in medium with glucose but poorly in medium with raffinose, and growth rates in medium with kestose differed between the strains. Oligosaccharide metabolism markedly influenced their LTA production, and apparent molecular size of LTA in electrophoresis recovered from cells cultured with glucose and kestose differed from that from cells cultured with raffinose in the strains. On the other hand, more than 15-fold more LTA was observed in the L. gasseri cells cultured with raffinose when compared with glucose or kestose after incubation for 15 h. Transcriptome analysis identified glycoside hydrolase family 32 enzyme as a potential kestose hydrolysis enzyme in the two strains. Transcriptomic levels of multiple genes in the dlt operon, involved in D-alanine substitution of LTA, were lower in cells cultured with raffinose than in those cultured with kestose or glucose. This suggested that the different sizes of LTA observed among the carbohydrates tested were partly due to different levels of alanylation of LTA. The present study indicates that available oligosaccharide has the impact on the LTA production of the industrially important lactobacilli, which might influence their probiotic properties.

scholarly journals Crystallographic analysis shows substrate binding at the −3 to +1 active-site subsites and at the surface of glycoside hydrolase family 11 endo-1,4-β-xylanases

2008 ◽  
Vol 410 (1) ◽  
pp. 71-79 ◽  
Author(s):  
Elien Vandermarliere ◽  
Tine M. Bourgois ◽  
Sigrid Rombouts ◽  
Steven van Campenhout ◽  
Guido Volckaert ◽  
...  
Keyword(s):  
Binding Site ◽  
Active Site ◽  
Glycoside Hydrolase ◽  
Plant Cell Wall ◽  
Substrate Binding ◽  
Crystallographic Analysis ◽  
Glycoside Hydrolase Family ◽  
Carbohydrate Binding ◽  
Carbohydrate Binding Modules ◽  
Hydrolase Family

GH 11 (glycoside hydrolase family 11) xylanases are predominant enzymes in the hydrolysis of heteroxylan, an abundant structural polysaccharide in the plant cell wall. To gain more insight into the protein–ligand interactions of the glycone as well as the aglycone subsites of these enzymes, catalytically incompetent mutants of the Bacillus subtilis and Aspergillus niger xylanases were crystallized, soaked with xylo-oligosaccharides and subjected to X-ray analysis. For both xylanases, there was clear density for xylose residues in the −1 and −2 subsites. In addition, for the B. subtilis xylanase, there was also density for xylose residues in the −3 and +1 subsite showing the spanning of the −1/+1 subsites. These results, together with the observation that some residues in the aglycone subsites clearly adopt a different conformation upon substrate binding, allowed us to identify the residues important for substrate binding in the aglycone subsites. In addition to substrate binding in the active site of the enzymes, the existence of an unproductive second ligand-binding site located on the surface of both the B. subtilis and A. niger xylanases was observed. This extra binding site may have a function similar to the separate carbohydrate-binding modules of other glycoside hydrolase families.

scholarly journals Genome-Wide Analysis of Glycoside Hydrolase Family 35 Genes and Their Potential Roles in Cell Wall Development in Medicago truncatula

Plants ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1639
Author(s):  
Junfeng Yang ◽  
Qian Li ◽  
Wenxuan Du ◽  
Yu Yao ◽  
Guoan Shen ◽  
...  
Keyword(s):  
Cell Wall ◽  
Medicago Truncatula ◽  
Glycoside Hydrolase ◽  
Expression Patterns ◽  
Functional Characterization ◽  
Glycoside Hydrolase Family ◽  
Forage Crops ◽  
Specific Expression ◽  
Hydrolase Family ◽  
Expression Module

Plant β-galactosidases (BGAL) function in various cell wall biogeneses and modifications, and they belong to the glycoside hydrolase family. However, the roles of BGAL family members in Medicago truncatula cell wall remodeling remain unclear. In this study, a total of 25 MtBGAL members of the glycoside hydrolase gene family 35 were identified, and they were clustered into nine sub-families. Many cis-acting elements possibly related to MeJA and abscisic acid responses were identified in the promoter region of the MtBGAL genes. Transcript analyses showed that these MtBGAL genes exhibited distinct expression patterns in various tissues and developing stem internodes. Furthermore, a stem-specific expression module associated with cell wall metabolic pathways was identified by weighted correlation network analysis (WGCNA). In particular, MtBGAL1 and MtBGAL23 within the stem-specific expression module were highly expressed in mature stems. In addition, several genes involved in lignin, cellulose, hemicellulose and pectin pathways were co-expressed with MtBGAL1 and MtBGAL23. It was also found that MtBGAL1 and MtBGAL23 were localized to the cell wall at the subcellular level, indicating their roles in the modification of cell wall metabolites in Medicago. As a whole, these results will be useful for further functional characterization and utilization of BGAL genes in cell wall modifications aiming to improve the quality of legume forage crops.

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