Analyzing structural features of proteins from deep-sea organisms.

Autor: Sieg J; Universität Hamburg, ZBH - Center for Bioinformatics, Hamburg, Germany., Sandmeier CC; Universität Hamburg, ZBH - Center for Bioinformatics, Hamburg, Germany., Lieske J; Deutsches Elektronen-Synchrotron DESY, Center for Free-Electron Laser Science, Hamburg, Germany., Meents A; Deutsches Elektronen-Synchrotron DESY, Center for Free-Electron Laser Science, Hamburg, Germany., Lemmen C; BioSolveIT GmbH, Sankt Augustin, Germany., Streit WR; Universität Hamburg, Department of Microbiology and Biotechnology, Hamburg, Germany., Rarey M; Universität Hamburg, ZBH - Center for Bioinformatics, Hamburg, Germany.
Jazyk: angličtina
Zdroj: Proteins [Proteins] 2022 Aug; Vol. 90 (8), pp. 1521-1537. Date of Electronic Publication: 2022 Apr 05.
DOI: 10.1002/prot.26337
Abstrakt: Protein adaptations to extreme environmental conditions are drivers in biotechnological process optimization and essential to unravel the molecular limits of life. Most proteins with such desirable adaptations are found in extremophilic organisms inhabiting extreme environments. The deep sea is such an environment and a promising resource that poses multiple extremes on its inhabitants. Conditions like high hydrostatic pressure and high or low temperature are prevalent and many deep-sea organisms tolerate multiple of these extremes. While molecular adaptations to high temperature are comparatively good described, adaptations to other extremes like high pressure are not well-understood yet. To fully unravel the molecular mechanisms of individual adaptations it is probably necessary to disentangle multifactorial adaptations. In this study, we evaluate differences of protein structures from deep-sea organisms and their respective related proteins from nondeep-sea organisms. We created a data collection of 1281 experimental protein structures from 25 deep-sea organisms and paired them with orthologous proteins. We exhaustively evaluate differences between the protein pairs with machine learning and Shapley values to determine characteristic differences in sequence and structure. The results show a reasonable discrimination of deep-sea and nondeep-sea proteins from which we distinguish correlations previously attributed to thermal stability from other signals potentially describing adaptions to high pressure. While some distinct correlations can be observed the overall picture appears intricate.
(© 2022 The Authors. Proteins: Structure, Function, and Bioinformatics published by Wiley Periodicals LLC.)
Databáze: MEDLINE
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