Microbial characterisation and Cold-Adapted Predicted Protein (CAPP) database construction from the active layer of Greenland’s permafrost

Permafrost represents a reservoir for the biodiscovery of cold-adapted proteins which are advantageous in industrial and medical settings. Comparisons between different thermo-adapted proteins can give important information for cold-adaptation bioengineering. We collected permafrost active layer sam...

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Bibliographic Details
Main Authors: Varliero, Gilda, Rafiq, Muhammad, Singh, Swati, Summerfield, Annabel, Sgouridis, Fotis, Cowan, Donald, Barker, Gary L A
Format: Article in Journal/Newspaper
Language:English
Published: 2021
Subjects:
Online Access:https://hdl.handle.net/1983/e653ef40-2c32-4f3d-a220-bc218a08a112
https://research-information.bris.ac.uk/en/publications/e653ef40-2c32-4f3d-a220-bc218a08a112
Description
Summary:Permafrost represents a reservoir for the biodiscovery of cold-adapted proteins which are advantageous in industrial and medical settings. Comparisons between different thermo-adapted proteins can give important information for cold-adaptation bioengineering. We collected permafrost active layer samples from 34 points along a proglacial transect in southwest Greenland. We obtained a deep read coverage assembly (>164x) from nanopore and Illumina sequences for the purposes of i) analysing metagenomic and metatranscriptomic trends of the microbial community of this area, and ii) creating the Cold-Adapted Predicted Protein (CAPP) database. The community showed a similar taxonomic composition in all samples along the transect, with a solid permafrost-shaped community, rather than microbial trends typical of proglacial systems. We retrieved 69 high- and medium-quality metagenome-assembled clusters, 213 complete biosynthetic gene clusters and more than three million predicted proteins. The latter constitute the CAPP database that can provide cold-adapted protein sequence information for protein- and taxon-focused amino acid sequence modifications for the future bioengineering of cold-adapted enzymes. As an example, we focused on the enzyme polyphenol oxidase, and demonstrated how sequence variation information could inform its protein engineering.