The modular evolution of chitinases is governed by coevolution of auxiliary and catalytic domains
Abstract
The modular architecture of multi-domain enzymes is a key source of functional diversity. GH18 chitinases exemplify this, possessing a variety of auxiliary domains that have been postulated to underpin their role as essential global nutrient cyclers. However, there is no evolutionary framework that accounts for the vast assortment of domain compositions observed across the protein family. Here, we map the sequence space of prokaryotic chitinases, integrating phylogenetics with a quantitative analysis of domain promiscuity to decode their evolutionary history. We reveal that diversification follows distinct trajectories: enzymes necessary for environmental chitin scavenging evolve via high modular plasticity and structural elaboration of the catalytic core, whereas sequences required for specialized, essential developmental roles fix their domain architecture to fulfil lineage-specific physiological roles. By resolving how domain accretion co-evolves with catalytic scaffolds, this work provides a framework for understanding how multi-domain enzymes adapt to complex environments.
Related
- Caenorhabditis elegans and Serratia marcescens host-parasite coevolution model strains derived through mutagenesis and experimental evolution
- Eukaryotic Mitogenomes and Their Key Insights: Architecture, Evolution, and Mitonuclear Coevolution
- Is Third Nature the Principal Internal Generative Driver of Human Gene–Culture Coevolution and Transgression? From Culture-Driven to Third-Nature-Driven Evolution: Brain Darwinian Machine–Culture Coevolution in Homo sapiens
- Harnessing catalytic knowledge to guide enzyme discovery and evolution with AlphaEnzyme
- Directed evolution of laccase from Thermus thermophilus HB27 reveals a variant with enhanced high temperature catalytic activity and electrochemical properties
BibTeX
@article{pulsford2026modular,
title = {{The modular evolution of chitinases is governed by coevolution of auxiliary and catalytic domains}},
author = {S. B. Pulsford and J. A. T. Dalton and O. B. Smith and J. Horton and R. L. Frkic and J. Z. Chen and J. Kaczmarski and C. J. Jackson},
journal = {Nature Communications},
year = {2026},
month = nov,
doi = {10.1038/s41467-026-79280-4},
url = {https://www.nature.com/articles/s41467-026-79280-4},
note = {CC BY 4.0},
}
RIS
TY - JOUR
TI - The modular evolution of chitinases is governed by coevolution of auxiliary and catalytic domains
AU - S. B. Pulsford
AU - J. A. T. Dalton
AU - O. B. Smith
AU - J. Horton
AU - R. L. Frkic
AU - J. Z. Chen
AU - J. Kaczmarski
AU - C. J. Jackson
PY - 2026
DA - 2026/11/05
JO - Nature Communications
DO - 10.1038/s41467-026-79280-4
UR - https://www.nature.com/articles/s41467-026-79280-4
AB - The modular architecture of multi-domain enzymes is a key source of functional diversity. GH18 chitinases exemplify this, possessing a variety of auxiliary domains that have been postulated to underpin their role as essential global nutrient cyclers. However, there is no evolutionary framework that accounts for the vast assortment of domain compositions observed across the protein family. Here, we map the sequence space of prokaryotic chitinases, integrating phylogenetics with a quantitative analysis of domain promiscuity to decode their evolutionary history. We reveal that diversification follows distinct trajectories: enzymes necessary for environmental chitin scavenging evolve via high modular plasticity and structural elaboration of the catalytic core, whereas sequences required for specialized, essential developmental roles fix their domain architecture to fulfil lineage-specific physiological roles. By resolving how domain accretion co-evolves with catalytic scaffolds, this work provides a framework for understanding how multi-domain enzymes adapt to complex environments.
SN - 2041-1723
ER -