The response of aminopeptidases of Phaseolus vulgaris to drought depends on the developmental stage of the leaves

作者: Maruška Budič , Blaž Cigić , Maja Šoštarič , Jerica Sabotič , Vladimir Meglič

DOI: 10.1016/J.PLAPHY.2016.10.007

关键词: LysinePhaseolusProteasesBiologyLeucinePMSFPlant physiologyPhenylalanineBotanyE-64

摘要: Aminopeptidases, together with other proteases, execute and regulate the total specifically limited protein breakdown involved in plant physiology, raising possibility of their involvement response to drought. We have identified, leaves Phaseolus vulgaris L., five aminopeptidases (E.C.3.4.11) whose levels activity changed when three week old plants were subjected First, second third trifoliate investigated separately. The first identified then isolated using ion exchange chromatography leaf extracts. Three, named PvAP1, PvAP2 PvAP4, are metallo broad substrate specificity, active against substrates conjugated alanine lysine. Two others, PvAP3 PvAP5, apparently serine aminopeptidases, former phenylalanine leucine, latter characterised by narrow specificity phenylalanine. Their apparent molecular weights range from ∼37 kDa ∼80 kDa. Levels individual both watered drought stressed shown depend on age leaves. In they generally highest young, very low older, leaves, exception PvAP5. Drought initiated an almost general increase activities, although different extents, PvAP4 PvAP5 young Thus, such studies it is necessary investigate effects separately ages order elucidate complex probably specific roles common bean

参考文章(39)
T. C. Elleman, Aminopeptidases of pea Biochemical Journal. ,vol. 141, pp. 113- 118 ,(1974) , 10.1042/BJ1410113
Zhiwei Cheng, Kun Dong, Pei Ge, Yanwei Bian, Liwei Dong, Xiong Deng, Xiaohui Li, Yueming Yan, Identification of Leaf Proteins Differentially Accumulated between Wheat Cultivars Distinct in Their Levels of Drought Tolerance. PLOS ONE. ,vol. 10, ,(2015) , 10.1371/JOURNAL.PONE.0125302
Bojana Vukelić, Ivica Strelec, Ljubinka Vitale, Aminopeptidases of Germinated and Non-Germinated Barley Food Technology and Biotechnology. ,vol. 47, pp. 296- 303 ,(2009)
Neil D Rawlings, Alan J Barrett, Robert Finn, None, Twenty years of the MEROPS database of proteolytic enzymes, their substrates and inhibitors Nucleic Acids Research. ,vol. 44, pp. 343- 350 ,(2016) , 10.1093/NAR/GKV1118
Wun S. Chao, Yong-Qiang Gu, Véronique Pautot, Elizabeth A. Bray, Linda L. Walling, Leucine aminopeptidase RNAs, proteins, and activities increase in response to water deficit, salinity, and the wound signals systemin, methyl jasmonate, and abscisic acid Plant Physiology. ,vol. 120, pp. 979- 992 ,(1999) , 10.1104/PP.120.4.979
Lyudmila Simova-Stoilova, Irina Vaseva, Biliana Grigorova, Klimentina Demirevska, Urs Feller, Proteolytic activity and cysteine protease expression in wheat leaves under severe soil drought and recovery. Plant Physiology and Biochemistry. ,vol. 48, pp. 200- 206 ,(2010) , 10.1016/J.PLAPHY.2009.11.003
Bartosz Oszywa, Maciej Makowski, Małgorzata Pawełczak, Purification and partial characterization of aminopeptidase from barley (Hordeum vulgare L.) seeds. Plant Physiology and Biochemistry. ,vol. 65, pp. 75- 80 ,(2013) , 10.1016/J.PLAPHY.2013.01.014
Inès Karmous, Abdelilah Chaoui, Khadija Jaouani, David Sheehan, Ezzedine El Ferjani, Valeria Scoccianti, Rita Crinelli, Role of the ubiquitin-proteasome pathway and some peptidases during seed germination and copper stress in bean cotyledons. Plant Physiology and Biochemistry. ,vol. 76, pp. 77- 85 ,(2014) , 10.1016/J.PLAPHY.2013.12.025
Maruška Budič, Marjetka Kidrič, Vladimir Meglič, Blaž Cigić, A quantitative technique for determining proteases and their substrate specificities and pH optima in crude enzyme extracts Analytical Biochemistry. ,vol. 388, pp. 56- 62 ,(2009) , 10.1016/J.AB.2009.01.045
Marjetka Kidrič, Jerica Sabotič, Branka Stevanović, Desiccation tolerance of the resurrection plant Ramonda serbica is associated with dehydration-dependent changes in levels of proteolytic activities. Journal of Plant Physiology. ,vol. 171, pp. 998- 1002 ,(2014) , 10.1016/J.JPLPH.2014.03.011