Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Damak, Naourez; Abdeljalil, Salma; Taeib, Noomen Hadj; Gargouri, Ali

doi:10.1007/s12010-015-1720-1

Cited by 5 publications

(3 citation statements)

References 36 publications

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“…N-glycosylation is employed as the shield to PsXEG1 from GmAP5 degradation [77,78]. Rhamnogalacturo-nan is a plant cell wall compound that can be hydrolyzed by rhamnogalacturonase, but it has received little attention [79].…”

Section: Discussionmentioning

confidence: 99%

Host Recognition and Specific Infection of Endomelanconiopsis endophytica during Early Infection

Xie,

Shi,

Cheng

et al. 2023

JoF

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Coevolution between the pathogen and host plant drives pathogenic effector diversity. However, the molecular mechanism behind host-specific pathogenesis remains to be explored. Here, we present a 43 Mb whole-genome sequence of Endomelanconiopsis endophytica strain LS29, a host-specific pathogen of the common subtropical tree Castanopsis fissa. We described its genome annotations and identified its effector candidates. By performing temporal transcriptome sequencing of E. endophytica on C. fissa during early infection, we found that E. endophytica repressed other microbes in order to attack the tissue of the host by producing antibiotics earlier than 24 h post-inoculation (hpi). Simultaneously, a variety of effectors were secreted to recognize the host plant, but most of them showed a significantly opposing expression regulation trend after 24 hpi, indicating that 24 hpi represents a key time point between host recognition and specific infection. Furthermore, a comparison of isoenzymes showed that only a few effectors were identified as specific effectors, which were involved in hydrolyzing the compounds of the plant cell wall and releasing fatty acids during the early infection of C. fissa. Our results determined host recognition timing and identified a specific catalog of effectors, which are crucial for revealing the molecular mechanism of host-specific pathogenesis.

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Section: Discussionmentioning

confidence: 99%

Host Recognition and Specific Infection of Endomelanconiopsis endophytica during Early Infection

Xie,

Shi,

Cheng

et al. 2023

JoF

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“…In contrast, exo-PGs have a closed-pocket active site that only binds to the non-reducing ends of pectins due to inserted stretches of amino acids ( Abbott and Boraston, 2007 ). Rhamno-PGs (RGs), which hydrolyze GalA-rhamnose bonds of rhamnogalacturonan-I, can be further divided into exo-RGs and endo-RGs ( Mutter et al, 1998 ; Choi et al, 2004 ; Damak et al, 2015 ). However, tertiary structures of exo-RGs remain unreported.…”

Section: Structural Characteristics and Classification Of Polygalactumentioning

confidence: 99%

A Profusion of Molecular Scissors for Pectins: Classification, Expression, and Functions of Plant Polygalacturonases

Yang

Liang

et al. 2018

Front. Plant Sci.

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In plants, the construction, differentiation, maturation, and degradation of the cell wall are essential for development. Pectins, which are major constituents of primary cell walls in eudicots, function in multiple developmental processes through their synthesis, modification, and degradation. Several pectin modifying enzymes regulate pectin degradation via different modes of action. Polygalacturonases (PGs), which function in the last step of pectin degradation, are a crucial class of pectin-modifying enzymes. Based on differences in their hydrolyzing activities, PGs can be divided into three main types: exo-PGs, endo-PGs, and rhamno-PGs. Their functions were initially investigated based on the expression patterns of PG genes and measurements of total PG activity in organs. In most plant species, PGs are encoded by a large, multigene family. However, due to the lack of genome sequencing data in early studies, the number of identified PG genes was initially limited. Little was initially known about the evolution and expression patterns of PG family members in different species. Furthermore, the functions of PGs in cell dynamics and developmental processes, as well as the regulatory pathways that govern these functions, are far from fully understood. In this review, we focus on how recent studies have begun to fill in these blanks. On the basis of identified PG family members in multiple species, we review their structural characteristics, classification, and molecular evolution in terms of plant phylogenetics. We also highlight the diverse expression patterns and biological functions of PGs during various developmental processes, as well as their mechanisms of action in cell dynamic processes. How PG functions are potentially regulated by hormones, transcription factors, environmental factors, pH and Ca2+ is discussed, indicating directions for future research into PG function and regulation.

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“…According to our previous work (Wang et al, 2014a), present arabinanase was an endo-acting type. Rhamnogalacturonase is an enzyme work on the "hairy region" of pectin, of which C4 of the backbone rhamnose residues is attached by multiple branching arabinan, galactan, and arabinogalactan side chains (Damak, Abdeljalil, Taeib, & Gargouri, 2015). Polygalacturonases is the enzyme hydrolyze the backbone of the smooth region of pectin, which is also acting in both exo-and endo-modes (De Vries & Visser, 2001).…”

Section: Optimization Of Ppase Productionmentioning

confidence: 99%

Protopectinase production byPaenibacillus polymyxaZ6 and its application in pectin extraction from apple pomace

Zhang

Zhao

Gao

et al. 2017

J Food Process Preserv

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Paenibacillus polymyxa Z6 was screened as protopectinase (PPase) producing strain and its PPase activity was 44.4 U/mL. The factors influencing PPase production were identified by a two-level Plackett-Burman design with seven variables. The results indicated that Ca 21 concentration, fermentation time, and temperature were the most influential factors on the PPase production, which were applied in the Box-Behnken design. The predicted maximum PPase activity was 219 U/mL and the experimental maximum PPase activity was 221 U/mL, under the predicted optimum conditions, 170 mg/L Ca 21, 27 8C, and 29 hr of fermentation. The present PPase was composed of both type-A PPase, polygalacturonase; and type-B PPase, arabinanase, and rhamnogalacturonase. Finally, the PPase was applied for the pectin extraction from apple pomace and achieved an average yield of 11.9% with properties like 8.5% moisture content, 1.6% ash content, 3.8 mPaÁS viscosity, and pH 6.1 of 1% solution. Practical applicationsProtopectinase (PPase) is a "green" way for pectin extraction with the advantages of low emission, rhamnogalacturonase. This PPase was used in pectin extraction from apple pomace and harvested pectin with lower moisture, lower ash, and higher viscosity compared with the chemically produced one, which indicates that this PPase has potential for application in food industry.

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Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Cited by 5 publications

References 36 publications

Host Recognition and Specific Infection of Endomelanconiopsis endophytica during Early Infection

Host Recognition and Specific Infection of Endomelanconiopsis endophytica during Early Infection

A Profusion of Molecular Scissors for Pectins: Classification, Expression, and Functions of Plant Polygalacturonases

Protopectinase production byPaenibacillus polymyxaZ6 and its application in pectin extraction from apple pomace

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