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alpha-Hydroxynitrile lyase protein from Xylella fastidiosa: Cloning, expression, and characterization.

Abstract：

:Xylella fastidiosa is a xylem-restricted plant pathogen that causes a range of diseases in several and important crops. Through comparative genomic sequence analysis many genes were identified and, among them, several potentially involved in plant-pathogen interaction. The experimental determination of the primary sequence of some markedly expressed proteins for X. fastidiosa and the comparison with the nucleic acids sequence of genome identified one of them as being SCJ21.16 (XFa0032) gene product. The comparative analysis of this protein against SWISSPROT database, in special, resulted in similarity with alpha-hydroxynitrile lyase enzyme (HNL) from Arabidopsis thaliana, causing interest for being one of the most abundant proteins both in the whole cell extract as well as in the extracellular protein fraction. It is known that HNL enzyme are involved in a process termed "cyanogenesis", which catalyzes the dissociation of alpha-hydroxinitrile into carbonyle and HCN when plant tissue is damaged. Although the complete genome sequences of X. fastidiosa are available and the cyanogenesis process is well known, the biological role of this protein in this organism is not yet functionally characterized. In this study we presented the cloning, expression, characterization of recombinant HNL from X. fastidiosa, and its probable function in the cellular metabolism. The successful cloning and heterologous expression in Escherichia coli resulted in a satisfactory amount of the recombinant HNL expressed in a soluble, and active form giving convenient access to pure enzyme for biochemical and structural studies. Finally, our results confirmed that the product of the gene XFa0032 can be positively assigned as FAD-independent HNLs.

journal_name

Microb Pathog

journal_title

Microbial pathogenesis

authors

Caruso CS,de Fátima Travensolo R,de Campus Bicudo R,de Macedo Lemos EG,Ulian de Araújo AP,Carrilho E

doi

10.1016/j.micpath.2009.06.007

subject

Has Abstract

pub_date

2009-09-01 00:00:00

pages

118-27

issue

3

eissn

0882-4010

issn

1096-1208

pii

S0882-4010(09)00090-4

journal_volume

47

pub_type

杂志文章

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