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嗜热自养甲烷杆菌对阿米洛利的抗性:膜相关蛋白的特性研究

Amiloride resistance in the methanoarcheon Methanothermobacter thermoautotrophicus: characterization of membrane-associated proteins.

作者信息

Surín S, Cubonová L', Majerník A I, Smigán P

机构信息

Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Ivanka pri Dunaji, Slovakia.

出版信息

Folia Microbiol (Praha). 2006;51(4):313-6. doi: 10.1007/BF02931822.

Abstract

An amiloride-resistant mutant with diminished Na+/H+ antiporter activity was isolated from Methanothermobacter thermoautotrophicus. To define the protein basis of amiloride resistance, the composition of membrane-associated proteins was partially characterized and compared with that of the wild type strain. An abundant 670-kDa membrane-associated protein that was present only in the mutant strain was analyzed by MALDI-TOF MS and identified as a coenzyme F420-reducing hydrogenase. The amiloride resistance was not accompanied by changes in protein size or changes in the level of subunits A or B of the A1A0-type ATP synthase; on the other hand, the SDS-PAGE patterns of the chloroform-methanol extract of membranes from both strains were different. Two bands with calculated molecular mass 16 and 11 kDa were identified as MtrD and AtpK, respectively. The observed over-expression of a 22.7-kDa protein in the mutant cells may represent the multimeric form of the MtrD subunit. These results show that the impairment of the Na+/H+ antiporter system in the amiloride-resistant mutant of Methanothermobacter thermoautotrophicus is accompanied by only small changes in a few membrane-associated proteins.

摘要

从嗜热自养甲烷杆菌中分离出一株对氨氯吡咪耐药的突变体,其Na⁺/H⁺逆向转运蛋白活性降低。为了确定氨氯吡咪耐药性的蛋白质基础,对膜相关蛋白的组成进行了部分表征,并与野生型菌株进行了比较。通过基质辅助激光解吸电离飞行时间质谱(MALDI-TOF MS)分析了仅存在于突变体菌株中的一种丰富的670 kDa膜相关蛋白,并鉴定为辅酶F420还原氢化酶。氨氯吡咪耐药性并未伴随着蛋白质大小的变化或A1A0型ATP合酶亚基A或B水平的变化;另一方面,两种菌株膜的氯仿-甲醇提取物的SDS-PAGE图谱不同。计算分子量为16 kDa和11 kDa的两条带分别被鉴定为MtrD和AtpK。在突变体细胞中观察到的22.7 kDa蛋白的过表达可能代表MtrD亚基的多聚体形式。这些结果表明,嗜热自养甲烷杆菌氨氯吡咪耐药突变体中Na⁺/H⁺逆向转运蛋白系统的损伤仅伴随着少数膜相关蛋白的微小变化。

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