Protein repeats evolve and emerge in giant viruses

Erdozain, Sofía; Barrionuevo, Emilia; Ripoll, Lucas; Mier, Pablo; Andrade‐Navarro, Miguel A.

doi:10.1016/j.jsb.2023.107962

Cited by 5 publications

(1 citation statement)

References 36 publications

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“…If both interacting partners are TRPs (or TRPs interact with an IDR), we could expect the evolutionary constraints to be much lower. Fast evolutionary rates of TRPs have been observed in giant viruses (e.g., ANK in the Acanthamoeba polyphaga mimivirus ; [ 45 ]); we would hypothesize that the function of these proteins is to interact with other TRPs or IDRs, or maybe not with any protein.…”

Section: Discussionmentioning

confidence: 99%

Structured Tandem Repeats in Protein Interactions

Mac Donagh,

Marchesini,

Spiga

et al. 2024

IJMS

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Tandem repeats (TRs) in protein sequences are consecutive, highly similar sequence motifs. Some types of TRs fold into structural units that pack together in ensembles, forming either an (open) elongated domain or a (closed) propeller, where the last unit of the ensemble packs against the first one. Here, we examine TR proteins (TRPs) to see how their sequence, structure, and evolutionary properties favor them for a function as mediators of protein interactions. Our observations suggest that TRPs bind other proteins using large, structured surfaces like globular domains; in particular, open-structured TR ensembles are favored by flexible termini and the possibility to tightly coil against their targets. While, intuitively, open ensembles of TRs seem prone to evolve due to their potential to accommodate insertions and deletions of units, these evolutionary events are unexpectedly rare, suggesting that they are advantageous for the emergence of the ancestral sequence but are early fixed. We hypothesize that their flexibility makes it easier for further proteins to adapt to interact with them, which would explain their large number of protein interactions. We provide insight into the properties of open TR ensembles, which make them scaffolds for alternative protein complexes to organize genes, RNA and proteins.

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Section: Discussionmentioning

confidence: 99%