Biological activity of ant nests in the middle taiga zone

Churilina, A. E.; Golichenkov, M. V.; Иванова, А. Е.; Zakalyukina, Yu. V.; Умаров, М. М.

doi:10.3103/s0147687417040020

Cited by 4 publications

(2 citation statements)

References 9 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“… 53 It is also conceivable that the GH18 enzymes have different temperature and pH optima, allowing the bacterium to degrade chitin under varying conditions. 54 Functional characterization of all the 29 chitinases, or of the 14 that were both detected and upregulated, could provide insight into the unique catalytic machinery of A. ripae . Notably, this will be a massive task, because several of these multidomain enzymes are likely difficult to express and assessment of synergistic effects between the many enzymes would be quite demanding.…”

Section: Resultsmentioning

confidence: 99%

“…It remains to be seen if the many different proteins are used to degrade chitin more efficiently or whether they reflect an ability to degrade a wider variety of chitin-containing (copolymeric) substrates, for example, including both chitin from the insect and from insect-associated fungi . It is also conceivable that the GH18 enzymes have different temperature and pH optima, allowing the bacterium to degrade chitin under varying conditions . Functional characterization of all the 29 chitinases, or of the 14 that were both detected and upregulated, could provide insight into the unique catalytic machinery of A. ripae .…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Genomic and Proteomic Study of Andreprevotia ripae Isolated from an Anthill Reveals an Extensive Repertoire of Chitinolytic Enzymes

et al. 2021

View full text Add to dashboard Cite

Chitin is an abundant natural polysaccharide that is hard to degrade because of its crystalline nature and because it is embedded in robust co-polymeric materials containing other polysaccharides, proteins, and minerals. Thus, it is of interest to study the enzymatic machineries of specialized microbes found in chitin-rich environments. We describe a genomic and proteomic analysis of Andreprevotia ripae , a chitinolytic Gram-negative bacterium isolated from an anthill. The genome of A. ripae encodes four secreted family GH19 chitinases of which two were detected and upregulated during growth on chitin. In addition, the genome encodes as many as 25 secreted GH18 chitinases, of which 17 were detected and 12 were upregulated during growth on chitin. Finally, the single lytic polysaccharide monooxygenase (LPMO) was strongly upregulated during growth on chitin. Whereas 66% of the 29 secreted chitinases contained two carbohydrate-binding modules (CBMs), this fraction was 93% (13 out of 14) for the upregulated chitinases, suggesting an important role for these CBMs. Next to an unprecedented multiplicity of upregulated chitinases, this study reveals several chitin-induced proteins that contain chitin-binding CBMs but lack a known catalytic function. These proteins are interesting targets for discovery of enzymes used by nature to convert chitin-rich biomass. The MS proteomic data have been deposited in the PRIDE database with accession number PXD025087.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%