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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.)

Biophysical and Structural Characterization of the Recombinant Human eIF3L

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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]
Total Authors: 8
[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
Total Affiliations: 6
Document type: Journal article
Source: PROTEIN AND PEPTIDE LETTERS; v. 21, n. 1, p. 56-62, JAN 2014.
Web of Science Citations: 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)

FAPESP's process: 09/01400-7 - Study of the interaction of NS4b of yellow fever virus and host cellular proteins
Grantee:Maurício Lacerda Nogueira
Support Opportunities: Regular Research Grants
FAPESP's process: 10/05043-1 - Characterization of the interaction of the NS5 protein of Yellow Fever with the human cellular protein eIF3L
Grantee:Ana Theresa Silveira de Morais
Support Opportunities: Scholarships in Brazil - Doctorate (Direct)