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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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

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Author(s):
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]
Total Authors: 8
Affiliation:
[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
Total Affiliations: 2
Document type: Journal article
Source: SCIENTIFIC REPORTS; v. 10, n. 1 JAN 29 2020.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 13/24705-3 - The filamentous fungus Neurospora crassa as a model organism for the functional characterization of proteins/transcription factors that regulate the carbohydrate metabolism
Grantee:Maria Celia Bertolini
Support Opportunities: Research Projects - Thematic Grants