Evolution based on domain combinations: the case of glutaredoxins |
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Authors: | Rui Alves Ester Vilaprinyo Albert Sorribas and Enrique Herrero |
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Institution: | (1) Departament de Ci?ncies M?diques B?siques, Universitat de Lleida, IRBLleida, Montserrat Roig 2, 25008 Lleida, Spain;(2) Institut d'Investigaci? Biom?dica de Bellvitge (IDIBELL), Hospitalet de Llobregat, Barcelona, Spain |
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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. |
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