Publications
The ISME journalJan 2025 |
19
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1
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DOI:
10.1093/ismejo/wraf121

Widespread distribution of bacteria containing PETases with a functional motif across global oceans

Alam, Intikhab; Marasco, Ramona; Momin, Afaque A; Aalismail, Nojood; Laiolo, Elisa; Martin, Cecilia; Sanz-Sáez, Isabel; Baltá Foix, Begoña; Sá, Elisabet L; Kamau, Allan; Guzmán-Vega, Francisco J; Jamil, Tahira; Acinas, Silvia G; Gasol, Josep M; Gojobori, Takashi; Agusti, Susana; Daffonchio, Daniele; Arold, Stefan T; Duarte, Carlos M
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Abstract
Accumulating evidence indicates that microorganisms respond to the ubiquitous plastic pollution by evolving plastic-degrading enzymes. However, the functional diversity of these enzymes and their distribution across the ocean, including the deep sea, remain poorly understood. By integrating bioinformatics and artificial intelligence-based structure prediction, we developed a structure- and function-informed algorithm to computationally distinguish functional polyethylene terephthalate-degrading enzymes (PETases) from variants lacking PETase activity (pseudo-PETase), either due to alternative substrate specificity or pseudogene origin. Through in vitro functional screening and in vivo microcosm experiments, we verified that this algorithm identified a high-confidence, searchable sequence motif for functional PETases capable of degrading PET. Metagenomic analysis of 415 ocean samples revealed 23 PETase variants, detected in nearly 80% of the samples. These PETases mainly occur between 1,000 and 2,000 m deep and at the surface in regions with high plastic pollution. Metatranscriptomic analysis further identified PETase variants that were actively transcribed by marine microorganisms. In contrast to their terrestrial counterparts-where PETases are taxonomically diverse-those in marine ecosystems were predominantly encoded and transcribed by members of the Pseudomonadales order. Our study underscores the widespread distribution of PETase-containing bacteria across carbon-limited marine ecosystems, identifying and distinguishing the PETase motif that underpins the functionality of these specialized cutinases.
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