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Type: Artigo de periódico
Title: Expression and purification of a small heat shock protein from the plant pathogen Xylella fastidiosa
Author: Azzoni, AR
Tada, SFS
Rosselli, LK
Paula, DP
Catani, CF
Sabino, AA
Barbosa, JARG
Guimaraes, BG
Eberlin, MN
Medrano, FJ
Souza, AP
Abstract: The small heat shock proteins (smHSPs) belong to a family of proteins that function as molecular chaperones by preventing protein aggregation and are also known to contain a conserved region termed a-crystallin domain. Here, we report the expression, purification, and partial characterization of a novel smHSP (HSP17.9) from the phytopathogen Xylella fastidiosa, causal agent of the citrus variegated chlorosis (CVC). The gene was cloned into a pET32-Xa/LIC vector to over-express the protein coupled with fusion tags in Escherichia coli BL21(DE3). The expressed HSP17.9 was purified by immobilized metal affinity chromatography (IMAC) and had its identity determined by mass spectrometry (MALDI-TOF). The correct folding of the purified recombinant protein was verified by circular dichroism spectroscopy. Finally, the HSP17.9 protein also proved to efficiently prevent induced aggregation of insulin, strongly indicating a chaperone-like activity. (C) 2003 Elsevier Inc. All rights reserved.
Subject: small heat shock protein
Xylella fastidiosa smHSP
expression and purification
Country: EUA
Editor: Academic Press Inc Elsevier Science
Citation: Protein Expression And Purification. Academic Press Inc Elsevier Science, v. 33, n. 2, n. 297, n. 303, 2004.
Rights: fechado
Identifier DOI: 10.1016/j.pep.2003.10.007
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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