{"title":"Superoxide Dismutase: A Differentiation Protein Expressed in Uromyces Germlings during Early Appressorium Development","authors":"J.S. Lamboy, R.C. Staples, H.C. Hoch","doi":"10.1006/emyc.1995.1035","DOIUrl":null,"url":null,"abstract":"<div><p>Lamboy, J. S., Staples, R. C., and Hoch H. C. 1995. Superoxide dismutase: A differentiation protein expressed in <em>Uromyces</em> germlings during early appressorium development. <em>Experimental Mycology</em> 19, 284-296. Germlings of the bean rust fungus <em>Uromyces appendiculatus</em> detect penetration sites on the surface of the host leaf by thigmosensing topographical features. Within 2-4 min after the apex of a urediospore germ tube encounters the cuticular lip of a stomate, the germling ceases polarized growth and begins to swell over the aperture. The mechanism by which the cells detect topographical signals is not understood; however, previous experiments indicated that the initiation process does not involve <em>de novo</em> gene expression. In order to detect posttranslational modifications, the protein profiles of induced and noninduced germlings were compared at the earliest stages of appressorium formation, and a 21-kDa differentiation protein was identified by a shift in isoelectric point. The N-terminal amino acid sequence exhibited homology with superoxide dismutase (SOD), and antibodies to a synthetic peptide fragment of the respective sequence recognized cooper/zinc isozymes of SOD in electroblots of native gels. Electroelution of the active enzyme bands and separation by SDS-PAGE indicated that the 21-kDa protein is a component of a tetrameric 85-kDa SOD.</p></div>","PeriodicalId":12110,"journal":{"name":"Experimental Mycology","volume":"19 4","pages":"Pages 284-296"},"PeriodicalIF":0.0000,"publicationDate":"1995-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1006/emyc.1995.1035","citationCount":"12","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Experimental Mycology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0147597585710353","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 12
Abstract
Lamboy, J. S., Staples, R. C., and Hoch H. C. 1995. Superoxide dismutase: A differentiation protein expressed in Uromyces germlings during early appressorium development. Experimental Mycology 19, 284-296. Germlings of the bean rust fungus Uromyces appendiculatus detect penetration sites on the surface of the host leaf by thigmosensing topographical features. Within 2-4 min after the apex of a urediospore germ tube encounters the cuticular lip of a stomate, the germling ceases polarized growth and begins to swell over the aperture. The mechanism by which the cells detect topographical signals is not understood; however, previous experiments indicated that the initiation process does not involve de novo gene expression. In order to detect posttranslational modifications, the protein profiles of induced and noninduced germlings were compared at the earliest stages of appressorium formation, and a 21-kDa differentiation protein was identified by a shift in isoelectric point. The N-terminal amino acid sequence exhibited homology with superoxide dismutase (SOD), and antibodies to a synthetic peptide fragment of the respective sequence recognized cooper/zinc isozymes of SOD in electroblots of native gels. Electroelution of the active enzyme bands and separation by SDS-PAGE indicated that the 21-kDa protein is a component of a tetrameric 85-kDa SOD.
Lamboy, J. S, Staples, R. C.和Hoch H. C. 1995。超氧化物歧化酶:一种在早期附着胞发育过程中表达的分化蛋白。真菌学通报,2009,28(4):387 - 398。摘要豆锈菌尾尾尾尾菌(Uromyces appendiculatus)的芽孢通过地形特征探测寄主叶片表面的渗透部位。在单孢子胚管顶端与气孔角质层唇接触后2 ~ 4分钟内,胚芽停止极化生长,开始向气孔上方膨胀。细胞检测地形信号的机制尚不清楚;然而,先前的实验表明,起始过程不涉及从头基因表达。为了检测翻译后修饰,我们比较了诱导和非诱导胚在附着胞形成的早期阶段的蛋白谱,并通过等电点的移位鉴定了一个21 kda的分化蛋白。n端氨基酸序列与超氧化物歧化酶(SOD)具有同源性,并且相应序列合成肽片段的抗体在天然凝胶的电印迹中识别SOD的铜/锌同工酶。电洗脱和SDS-PAGE分离表明,21 kda蛋白是85-kDa四聚体SOD的一个组成部分。