| Texto completo | |
| Autor(es): |
Lopes, Gabriel Sarti
[1]
;
Paula Lico, Diego Torrecillas
[1]
;
Silva-Rocha, Rafael
[1]
;
de Oliveira, Renata Rocha
[2]
;
Sebollela, Adriano
[3]
;
Paco-Larson, Maria Luisa
[1]
;
Larson, Roy Edward
[1]
Número total de Autores: 7
|
| Afiliação do(s) autor(es): | [1] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Cellular & Mol Biol, BR-14049900 Sao Paulo - Brazil
[2] Natl Lab Biosci LNBio CNPEM, BR-13083970 Campinas, SP - Brazil
[3] Univ Sao Paulo, Ribeirao Preto Med Sch, Dept Biochem & Immunol, BR-14049900 Sao Paulo - Brazil
Número total de Afiliações: 3
|
| Tipo de documento: | Artigo Científico |
| Fonte: | Neuroscience Letters; v. 696, p. 219-224, MAR 23 2019. |
| Citações Web of Science: | 1 |
| Resumo | |
Eukaryotic mRNA precursors are co-transcriptionally assembled into ribonucleoprotein complexes. Heterogeneous nuclear ribonucleoprotein (hnRNP) complexes are involved in mRNA translocation, stability, subcellular localization and regulation of mRNA translation. About 20 major classes of hnRNPs have been identified in mammals. In a previous work, we characterized a novel, strongly-basic, RNA-binding protein (p65) in presynaptic terminals of squid neurons presenting homology with human hnRNPA/B type proteins, likely involved in local mRNA processing. We have identified and sequenced two hnRNPA/B-like proteins associated with tissue purified squid p65: Protein 1 (36.3 kDa, IP 7.1) and Protein 2 (37.6 kDa, IP 8.9). In the present work we generated an in silico, tridimensional, structural model of squid hnRNPA/B-like Protein 2, which showed highly conserved secondary and tertiary structure of RNA recognition motifs with human hnRNPA1 protein, as well as illustrated the potential for squid Protein 2 stable homodimerization. This was supported by biophysical measurements of bacterially expressed, recombinant protein. In addition, we induced expression of squid hnRNPA/B-like Protein 2 in human neuroblastoma cells (SH-SY5Y) and observed an exclusively nuclear localization, which depended on an intact C-terminal amino acid sequence and which relocated to cytoplasm particles containing PABP when the cells were challenged with sorbitol, suggesting an involvement with stress granule function. (AU) | |
| Processo FAPESP: | 04/08868-0 - Consolidação do Centro de Microscopia Funcional do Campus da USP/ Ribeirão Preto |
| Beneficiário: | Roy Edward Larson |
| Modalidade de apoio: | Auxílio à Pesquisa - Programa Equipamentos Multiusuários |