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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Comparative study of the interactions between fungal transcription factor nuclear localization sequences with mammalian and fungal importin-alpha

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Autor(es):
Bernardes, Natalia E. [1] ; Fukuda, Cintia A. [1] ; da Silva, Taina D. [1] ; de Oliveira, Hamine C. [1] ; de Barros, Andrea C. [1] ; Dreyer, Thiago R. [1] ; Bertolini, Maria Celia [2] ; Fontes, Marcos R. M. [1]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Univ Estadual Paulista UNESP, Inst Biociencias, Dept Fis & Biofis, Botucatu, SP - Brazil
[2] Univ Estadual Paulista UNESP, Inst Quim, Dept Bioquim & Tecnol Quim, Araraquara, SP - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: SCIENTIFIC REPORTS; v. 10, n. 1 JAN 29 2020.
Citações Web of Science: 0
Resumo

Importin-alpha (Imp alpha) is an adaptor protein that binds to cargo proteins (containing Nuclear Localization Sequences - NLSs), for their translocation to the nucleus. The specificities of the Imp alpha /NLS interactions have been studied, since these features could be used as important tools to find potential NLSs in nuclear proteins or even for the development of targets to inhibit nuclear import or to design peptides for drug delivery. Few structural studies have compared different Imp alpha variants from the same organism or Imp alpha of different organisms. Previously, we investigated nuclear transport of transcription factors with Neurospora crassa Imp alpha (NcImp alpha). Herein, NIT-2 and PAC-3 transcription factors NLSs were studied in complex with Mus musculus Imp alpha (MmImp alpha). Calorimetric assays demonstrated that the PAC-3 NLS peptide interacts with both Imp alpha proteins with approximately the same affinity. The NIT-2 NLS sequence binds with high affinity to the Imp alpha major binding site from both organisms, but its binding to minor binding sites reveals interesting differences due to the presence of additional interactions of NIT-2-NLS with MmImp alpha. These findings, together with previous results with Imp alpha from other organisms, indicate that the differential affinity of NLSs to minor binding sites may be also responsible for the selectivity of some cargo proteins recognition and transport. (AU)

Processo FAPESP: 13/24705-3 - O fungo filamentoso Neurospora crassa como um organismo modelo para a caracterização funcional de proteínas/fatores de transcrição que regulam o metabolismo de carboidratos
Beneficiário:Maria Celia Bertolini
Modalidade de apoio: Auxílio à Pesquisa - Temático