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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.)

Biophysical and Structural Characterization of the Recombinant Human eIF3L

Morais, Ana T. S. [1, 2] ; Meza, Andreia N. [3] ; Araujo, Gabriela C. [4, 5] ; Vidotto, Alessandra [1] ; Souza, Fatima P. [4, 5] ; Fossey, Marcelo A. [4, 5] ; Murakami, Mario T. [3] ; Nogueira, Mauricio L. [1, 6]
Número total de Autores: 8
Afiliação do(s) autor(es):
[1] Fac Med Sao Jose do Rio Preto FAMERP, Dept Doencas Dermat Infecciosas & Parasitarias, Lab Pesquisas Virol, BR-15090000 Sao Jose Do Rio Preto, SP - Brazil
[2] Univ Estadual Paulista, Dept Biol, IBILCE UNESP, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[3] CNPEM, LNBio, Lab Nacl Biociencias, BR-13083970 Campinas, SP - Brazil
[4] Univ Estadual Paulista, Dept Fis, IBILCE UNESP, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[5] Univ Estadual Paulista, Lab Multiusuario Inovacao Bio Mol, Sao Jose de Rio Preto IBILCE UNESP, BR-15054000 Sao Jose Do Rio Preto, SP - Brazil
[6] Univ Texas Med Branch, Ctr Trop Dis, Galveston, TX 77555 - USA
Número total de Afiliações: 6
Tipo de documento: Artigo Científico
Fonte: PROTEIN AND PEPTIDE LETTERS; v. 21, n. 1, p. 56-62, JAN 2014.
Citações Web of Science: 2

The eukaryotic translation initiation factor 3, subunit L (eIF3L) is one of the subunits of the eIF3 complex, an accessory protein of the Polymerase I enzyme and may have an important role in the Flavivirus replication by interaction with a viral non-structural 5 protein. Considering the importance of eIF3L in a diversity of cellular functions, we have produced the recombinant full-length eIF3L protein in Escherichia coli and performed spectroscopic and in silico analyses to gain insights into its hydrodynamic behavior and structure. Dynamic light scattering showed that eIF3L behaves as monomer when it is not interacting with other molecular partners. Circular dichroism experiments showed a typical spectrum of alpha-helical protein for eIF3L, which is supported by sequence-based predictions of secondary structure and the 3D in silico model. The molecular docking with the K subunit of the eIF3 complex revealed a strong interaction. It was also predicted several potential interaction sites in eIF3L, indicating that the protein is likely capable of interacting with other molecules as experimentally shown in other functional studies. Moreover, bioinformatics analyses showed approximately 8 putative phosphorylation sites and one possible N-glycosylation site, suggesting its regulation by post-translational modifications. The production of the eIF3L protein in E. coli and structural information gained in this study can be instrumental for target-based drug design and inhibitors against Flavivirus replication and to shed light on the molecular mechanisms involved in the eukaryotic translation initiation. (AU)

Processo FAPESP: 09/01400-7 - Estudo das interações entre a proteína NS4B do vírus da febre amarela e proteínas celulares
Beneficiário:Maurício Lacerda Nogueira
Linha de fomento: Auxílio à Pesquisa - Regular
Processo FAPESP: 10/05043-1 - Caracterização da interação entre proteínas não estruturais do vírus da Febre Amarela e eIF3L
Beneficiário:Ana Theresa Silveira de Morais
Linha de fomento: Bolsas no Brasil - Doutorado Direto