Evolution Based on Domain Combinations: the Case of Glutaredoxins

Overview

Journal BMC Evol Biol

Publisher Biomed Central

Specialty Biology

Date 2009 Mar 27

PMID 19321008

Citations 15

Authors

Rui Alves

Ester Vilaprinyo

Albert Sorribas

Enrique Herrero

Affiliations

Soon will be listed here.

Abstract

Background: Protein domains represent the basic units in the evolution of proteins. Domain duplication and shuffling by recombination and fusion, followed by divergence are the most common mechanisms in this process. Such domain fusion and recombination events are predicted to occur only once for a given multidomain architecture. However, other scenarios may be relevant in the evolution of specific proteins, such as convergent evolution of multidomain architectures. With this in mind, we study glutaredoxin (GRX) domains, because these domains of approximately one hundred amino acids are widespread in archaea, bacteria and eukaryotes and participate in fusion proteins. GRXs are responsible for the reduction of protein disulfides or glutathione-protein mixed disulfides and are involved in cellular redox regulation, although their specific roles and targets are often unclear.

Results: In this work we analyze the distribution and evolution of GRX proteins in archaea, bacteria and eukaryotes. We study over one thousand GRX proteins, each containing at least one GRX domain, from hundreds of different organisms and trace the origin and evolution of the GRX domain within the tree of life.

Conclusion: Our results suggest that single domain GRX proteins of the CGFS and CPYC classes have, each, evolved through duplication and divergence from one initial gene that was present in the last common ancestor of all organisms. Remarkably, we identify a case of convergent evolution in domain architecture that involves the GRX domain. Two independent recombination events of a TRX domain to a GRX domain are likely to have occurred, which is an exception to the dominant mechanism of domain architecture evolution.

Citing Articles

Unraveling the roles of aromatic cluster side-chain interactions on the structural stability and functional significance of psychrophilic Sphingomonas sp. glutaredoxin 3.

Tran T, Hoang T, Jang S, Lee C PLoS One. 2023; 18(8):e0290686.

PMID: 37651358 PMC: 10470887. DOI: 10.1371/journal.pone.0290686.

Relationships between the Reversible Oxidation of the Single Cysteine Residue and the Physiological Function of the Mitochondrial Glutaredoxin S15 from .

Christ L, Couturier J, Rouhier N Antioxidants (Basel). 2023; 12(1).

PMID: 36670964 PMC: 9854632. DOI: 10.3390/antiox12010102.

Glutathione Metabolism in Plants under Stress: Beyond Reactive Oxygen Species Detoxification.

Dorion S, Ouellet J, Rivoal J Metabolites. 2021; 11(9).

PMID: 34564457 PMC: 8464934. DOI: 10.3390/metabo11090641.

Antioxidant ability of glutaredoxins and their role in symbiotic nitrogen fixation in bv. 3841.

Zou Q, Zhou Y, Cheng G, Peng Y, Luo S, Wu H Appl Environ Microbiol. 2020; 87(4).

PMID: 33277272 PMC: 7851698. DOI: 10.1128/AEM.01956-20.

Glutaredoxin represses transcriptional and developmental responses to nitrate in roots.

Ehrary A, Rosas M, Carpinelli S, Davalos O, Cowling C, Fernandez F Plant Direct. 2020; 4(6):e00227.

PMID: 32537558 PMC: 7287413. DOI: 10.1002/pld3.227.

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