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Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli.

Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Research Abstract Details 

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  • Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Abstract Text:

    xiaoyu wangXiaoyu Wang,ming liMing Li,jiahuan zhangJiahuan Zhang,yan zhangYan Zhang,guiying zhangGuiying Zhang,jinsheng wangJinsheng Wang,xiaoyu wangXiaoyu Wang,ming liMing Li,jiahuan zhangJiahuan Zhang,yan zhangYan Zhang,guiying zhangGuiying Zhang,jinsheng wangJinsheng Wang,

    In the current study, we identified a key functional region in harpins from Xanthomonas that suppressed protein aggregation and mediated its expression in E. coli. Our data suggested that the presence of two common features in harpins [Wei et al. (1992) Science 257:85-88], namely, high glycine content and lack of cysteine residues, were not sufficient for Xanthomonas to elicit hypersensitive response (HR) activity or heat stability. Additionally, bioinformatic analyses revealed that the secondary structure of a conserved N-terminal region consisting of 12 highly hydrophilic amino acids (QGISEKQLDQLL) was alpha-helical. Following site-directed mutagenesis deletion of this region, the three mutated harpin proteins, in cultures induced at 37 degrees C, failed to elicit a HR in tobacco leaves. However, at 24 degrees C, two mutated harpins retained the ability to elicit HR, albeit with lower expression levels than that noted with the wild-type. SDS-PAGE and Western blot data suggested the HpaG mutant protein was found almost entirely in the inclusion body. These data demonstrated that these conserved amino acid residues played a critical role in protein aggregation and inclusion body formation in harpins from Xanthomonas.

    Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Publishing Authors By Initials

    x wangX Wang,m liM Li,j zhangJ Zhang,y zhangY Zhang,g zhangG Zhang,j wangJ Wang,x wangX Wang,m liM Li,j zhangJ Zhang,y zhangY Zhang,g zhangG Zhang,j wangJ Wang,

    For similar abstracts research abstracts see: abstracts research

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    Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Molecular biology reports

    VOLUME: 34

    Page Numbers: 189-98

    Journal Abbreviation: Mol. Biol. Rep.

    ISSN: 0301-4851

    DAY: 19

    MONTH: 12

    YEAR: 2006

    Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Information

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    LANGUAGE: eng

    NlmUniqueID: 403234

    Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli. Keywords Mesh Terms:

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    Grant and Affiliation Information for Identification of a key functional region in harpins from Xanthomonas that suppresses protein aggregation and mediates harpin expression in E. coli.

    AFFILIATION: Department of Plant Pathology, Nanjing Agricultural University, Nanjing, China.

    Country: Netherlands

    Netherlands Research PublicationNetherlands Research Publication

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    MEDLINETA: Mol Biol Rep

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