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New lives for old: evolution of pseudoenzyme function illustrated by iRhoms
Colin Adrain1, Matthew Freeman
1Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Nature Reviews. Molecular Cell Biology
|July 12, 2012
Summary
Inactive enzymes, or pseudoenzymes, are evolutionarily conserved and play crucial roles in regulating protein pathways. Studying these overlooked
Area of Science:
- Biochemistry
- Evolutionary Biology
- Molecular Biology
Background:
- Genomic sequencing reveals that many enzyme families contain inactive homologues, termed pseudoenzymes.
- The conservation of pseudoenzymes suggests they possess significant biological functions.
- Pseudoenzymes have been largely overlooked despite their evolutionary importance.
Purpose of the Study:
- To explore the mechanistic insights and evolutionary significance of 'dead' enzymes.
- To highlight the regulatory roles of pseudoenzymes within cellular pathways.
Main Methods:
- Analysis of large-scale genomic sequencing data.
- Comparative genomics to identify conserved pseudoenzymes.
- Functional characterization of specific pseudoenzyme families, including iRhoms.
Main Results:
- Identified numerous conserved pseudoenzymes across various enzyme families.
- Demonstrated that inactive rhomboid protease homologues (iRhoms) regulate protein trafficking in the secretory pathway.
- iRhoms, along with derlins and other rhomboid-like proteins, are key regulators of protein fate.
Conclusions:
- Pseudoenzymes are not evolutionary relics but possess critical functions.
- These 'dead' enzymes represent a significant, underappreciated source of biological regulators.
- Further investigation into pseudoenzymes can yield novel insights into cellular processes and potential therapeutic targets.
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