Bioinformatic mapping of a more precise Aspergillus niger degradome

Abstract

Aspergillus niger has the ability to produce a large variety of proteases, which are of particular importance for protein digestion, intracellular protein turnover, cell signaling, flavour development, extracellular matrix remodeling and microbial defense. However, the A. niger degradome (the full repertoire of peptidases encoded by the A. niger genome) available is not accurate and comprehensive. Herein, we have utilized annotations of A. niger proteases in AspGD, JGI, and version 12.2 MEROPS database to compile an index of at least 232 putative proteases that are distributed into the 71 families/subfamilies and 26 clans of the 6 known catalytic classes, which represents ~ 1.64% of the 14,165 putative A. niger protein content. The composition of the A. niger degradome comprises ~ 7.3% aspartic, ~ 2.2% glutamic, ~ 6.0% threonine, ~ 17.7% cysteine, ~ 31.0% serine, and ~ 35.8% metallopeptidases. One hundred and two proteases have been reassigned into the above six classes, while the active sites and/or metal-binding residues of 110 proteases were recharacterized. The probable physiological functions and active site architectures of these peptidases were also investigated. This work provides a more precise overview of the complete degradome of A. niger, which will no doubt constitute a valuable resource and starting point for further experimental studies on the biochemical characterization and physiological roles of these proteases.

Beneficial bacterial-Auricularia cornea interactions fostering growth enhancement identified from microbiota present in spent mushroom substrate

“…On the other hand, the increase in metallo-peptidases most likely helps in matrix remodeling, or microbial defense (Dong et al, 2021). Among the most abundant peptidases of A. cornea, the numbers of serine proteases markedly increased in the co-culture condition, compared to the single-culture conditions.…”

“…Interestingly, the numbers of cysteine- and metallo-peptidases of P. mangrovi increased significantly in the co-culture condition, compared to the single-culture conditions. The increase in the numbers of cysteine-proteases may help better protein turnover regulation and cellular homeostasis regulation ( Dong et al, 2021 ). On the other hand, the increase in metallo-peptidases most likely helps in matrix remodeling, or microbial defense ( Dong et al, 2021 ).…”

“…The increase in the numbers of cysteine-proteases may help better protein turnover regulation and cellular homeostasis regulation ( Dong et al, 2021 ). On the other hand, the increase in metallo-peptidases most likely helps in matrix remodeling, or microbial defense ( Dong et al, 2021 ). Among the most abundant peptidases of A. cornea , the numbers of serine proteases markedly increased in the co-culture condition, compared to the single-culture conditions.…”

Assessment of Post-Radiation Time Effect on Gene Expression Profiles of Saccharomyces cerevisiae Samples After Appling a UV Laser

“…PRN11 is a 26S proteasome regulatory subunit 19 ; this metalloisopeptidase hydrolyzes the ubiquitin molecule which is transported to the proteasome for degradation. 20 Investigations have revealed that UBI4 deletion leads to stopped accumulation of ubiquitin, cell tolerance reduction to some stresses such as oxidative, osmotic, cell wall perturbing and heat-shock stresses.…”

Genomic Characterization of Parengyodontium torokii sp. nov., a Biofilm-Forming Fungus Isolated from Mars 2020 Assembly Facility

“…More specifically, enzymes of the M24B family cleavage the N-terminal amino acid from peptides harboring a proline residue at the second position and are essential for cellular metabolic processes [94]. The members of the M28E family are characterized as aminopeptidases that are important for protein turnover and virulence [95,96]. Lastly, the function of metalloprotease belonging to the family M35 has been widely investigated in fungal genomes [76].…”