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从人类致病性头状芽裂酵母的酵母和菌丝形态中鉴定出一种具有谷胱甘肽转移酶活性的延伸因子1Bγ蛋白。

Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatus.

作者信息

Allocati Nerino, Masulli Michele, Del Boccio Piero, Pieragostino Damiana, D'Antonio Domenico, Sheehan David, Di Ilio Carmine

机构信息

Department of Experimental and Clinical Sciences, University "G. d'Annunzio", Via dei Vestini, 66013, Chieti, Italy,

出版信息

Folia Microbiol (Praha). 2014 Mar;59(2):107-13. doi: 10.1007/s12223-013-0273-3. Epub 2013 Aug 3.

DOI:10.1007/s12223-013-0273-3
PMID:23913100
Abstract

Blastoschizomyces capitatus is an uncommon, opportunistic pathogenic fungus, which causes invasive and disseminated infections. This microorganism is normally present in both environmental and normal human flora. Within a host, B. capitatus is able to grow in both unicellular yeast and multicellular filamentous growth forms. In this study, we obtained in vitro morphological conversion of B. capitatus from yeast-to-mycelial phase to investigate the presence and expression of glutathione transferase (GST) enzymes in both cell forms. A protein with GST activity using the model substrate 1-chloro-2,4-dinitrobenzene was detected in both morphologies and identified by tandem mass spectrometry as a eukaryotic elongation factor 1Bγ (eEF1Bγ) protein, a member of the GST superfamily. No significant difference in GST-specific activity and kinetic constants were observed between mycelial and yeast forms, indicating that eEF1Bγ protein did not show differential expression between the two phases.

摘要

头裂芽殖酵母是一种不常见的机会致病性真菌,可引起侵袭性和播散性感染。这种微生物通常存在于环境和正常人体菌群中。在宿主体内,头裂芽殖酵母能够以单细胞酵母和多细胞丝状生长形式生长。在本研究中,我们对头裂芽殖酵母进行了体外形态转化,从酵母期转变为菌丝期,以研究两种细胞形式中谷胱甘肽转移酶(GST)酶的存在和表达。使用模型底物1-氯-2,4-二硝基苯检测到具有GST活性的蛋白质,两种形态均有该蛋白,并通过串联质谱鉴定为真核延伸因子1Bγ(eEF1Bγ)蛋白,它是GST超家族的成员。在菌丝体和酵母形式之间未观察到GST比活性和动力学常数的显著差异,这表明eEF1Bγ蛋白在两个阶段之间未表现出差异表达。

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The role of glutathione S-transferase GliG in gliotoxin biosynthesis in Aspergillus fumigatus.
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