Article
Diversity and genome mapping assessment of disordered and functional domains in trypanosomatids
Registro en:
AVELAR, Grace Santos Tavares et al. Diversity and genome mapping assessment of disordered and functional domains in trypanosomatids. Journal of Proteomics, v. 227, 10391, 2020
1874-3919
10.1016/j.jprot.2020.103919
Autor
Avelar, Grace Santos Tavares
Gonçalves, Leilane Oliveira
Guimarães, Frederico Gonçalves
Guimarães, Paul Anderson Souza
Rocha, Luiz Gustavo do Nascimento
Carvalho, Maria Gabriela Reis
Resende, Daniela de Melo
Ruiz, Jeronimo Conceição
Resumen
The proteins that have structural disorder exemplify a class of proteins which is part of a new frontier in structural biology that demands a new understanding of the paradigm of structure/function correlations. In order to address the location, relative distances and the functional/structural correlation between disordered and conserved domains, consensus disordered predictions were mapped together with CDD domains in Leishmania braziliensis M2904, Leishmania infantum JPCM5, Trypanosoma cruzi CL-Brener Esmeraldo-like, Trypanosoma cruzi Dm28c, Trypanosoma cruzi Sylvio X10, Blechomonas ayalai B08-376 and Paratrypanosoma confusum CUL13 predicted proteomes. Our results depicts the role of protein disorder in key aspects of parasites biology highlighting: a) statistical significant association between genome structural location of protein disordered consensus stretches and functional domains; b) that disordered protein stretches appear in greater percentage at upstream or downstream position of the predicted domain; c) a possible role of structural disorder in several gene expression, control points that includes but are not limited to: i) protein folding; ii) protein transport and degradation; and iii) protein modification. In addition, for values of protein with disorder content greater than 40%, a small percentage of protein binding sites in IDPs/IDRs, a higher hypothetical protein annotation frequency was observed than expected by chance and trypanosomatid multigene families linked with virulence are rich in protein with disorder content.