Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms

Gir2 is an intrinsically unstructured protein that is present in Saccharomyces cerevisiae as a group of heterogeneously electrophoretic migrating forms

Autor Alves, V. S. Google Scholar
Castilho, B. A. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Resumo Gir2 is a highly acidic cytoplasmic protein of Saccharomyces cerevisiae of unknown function that shows an anomalous migration on SDS-PAGE. Based on its large Stokes radius and thermostability, we have previously suggested that Gir2 lacks extensive secondary structure. Here we report that Gir2 is extremely sensitive to proteolysis when compared to glutathione-S-transferase, a highly structured protein, further indicating its unfolded nature. Prediction based on the FoldIndex program also indicates that Gir2 is a disordered protein. Using truncated forms of Gir2 we show that the N-terminal half of this protein, with its high content of acidic amino acid residues, is responsible for the anomalous electrophoretic behavior of Gir2. Because all these features are hallmarks of intrinsically unstructured proteins (IUP), we propose that Gir2 is another representative of the IUP group of proteins. Additionally, we describe that the endogenous yeast Gir2 shows heterogeneous electrophoretic mobility, which is not due to proteolytic cleavage. (C) 2005 Elsevier Inc. All rights reserved.
Palavra-chave Gir2
natively unfolded
intrinsically unstructured protein
limited proteolysis
Idioma Inglês
Data de publicação 2005-07-01
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 332, n. 2, p. 450-455, 2005.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 450-455
Fonte http://dx.doi.org/10.1016/j.bbrc.2005.04.151
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000229572300021
Endereço permanente http://repositorio.unifesp.br/handle/11600/28368

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