NDLI: Harmaline-resistant mutant of Methanothermobacter thermautotrophicus with a lesion in Na(+)/H(+) antiport.

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Harmaline-resistant mutant of Methanothermobacter thermautotrophicus with a lesion in Na(+)/H(+) antiport.

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Harmaline-resistant mutant of Methanothermobacter thermautotrophicus with a lesion in Na(+)/H(+) antiport.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Vidová, Monika Bobálová, Janette Smigán, Peter
Description	Author Affiliation: Vidová M ( Institute of Animal Biochemistry and Genetics, Slovak Academy of Sciences, Moyzesova 61, 900 28 Ivanka pri Dunaji, Slovak Republic.)
Abstract	A spontaneous mutant of Methanothermobacter thermautotrophicus resistant to the Na(+)/H(+) antiporter inhibitor harmaline was isolated. The Na(+)/H(+) exchange activity in the mutant cells was remarkably decreased in comparison with wild-type cells. Na(+)/H(+) antiport activity of wild-type cells grown in the high Na(+) concentration (125 mmol/l) was significantly increased as compared to the cells grown under low Na(+) concentration (6.25 mmol/l) conditions. In contrast, harmaline resistant mutant showed almost the same Na(+)/H(+) antiport activity under both these conditions. While harmaline profoundly inhibited methanogenesis in the wild-type, increased methanogenesis was observed both in the presence and absence of harmaline in the mutant strain. ATP synthesis driven by methanogenic electron transport was significantly enhanced in the mutant cells. The experimental data revealed the differential expression of A flavoprotein and molybdenum-containing formylmethanofuran dehydrogenase 1 subunit C in harmaline-resistant mutant. The overexpression of these proteins might contribute to harmaline resistance. Taken together the results indicate that harmaline resistance in this mutant has arisen as a consequence of mutation(s) in antiporter gene(s) or protein(s) linked to antiporter activity. Moreover this work provides the evidence that Na(+)/H(+) exchanger deficiency in harmaline-resistant mutant can induce overexpression of several proteins participating in methanogenesis.
File Format	HTM / HTML
ISSN	02315882
e-ISSN	13384325
Journal	General physiology and biophysics
Volume Number	30 Spec No
Language	English
Publisher	Ústav molekulárnej fyziológie a genetiky SAV
Publisher Date	2011-01-01
Publisher Place	Slovak Republic
Access Restriction	Open
Subject Keyword	Discipline Physiology Discipline Biophysics Drug Resistance Genetics Harmaline Pharmacology Methanobacteriaceae Drug Effects Mutation Sodium-hydrogen Antiporter Metabolism Adenosine Triphosphate Biosynthesis Gene Expression Regulation, Archaeal Methane Growth & Development Potassium Salicylanilides Antagonists & Inhibitors Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Physiology Medicine Biophysics

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