Selective extraction of subunit D of the Na+-translocating methyltransferase and subunit c of the A(1)A(0) ATPase from the cytoplasmic membrane of methanogenic archaea by chloroform/methanol and characterization of subunit c of Methanothermobacter thermoautotrophicus as a 16-kDa proteolipid

Autor(en): Ruppert, C
Schmid, R
Hedderich, R
Muller, V
Stichwörter: A(1)A(0) ATPase; archaeon; CLONING; coenzyme M methyltransferase; EXPRESSION; GENES; GROWTH; METHANOBACTERIUM-THERMOAUTOTROPHICUM; METHANOSARCINA-MAZEI GO1; methyltetrahydromethanopterin; Microbiology; N-5-METHYLTETRAHYDROMETHANOPTERIN-COENZYME-M METHYLTRANSFERASE; proteolipid; SYNTHASE
Erscheinungsdatum: 2001
Herausgeber: ELSEVIER SCIENCE BV
Enthalten in: FEMS MICROBIOLOGY LETTERS
Band: 195
Ausgabe: 1
Startseite: 47
Seitenende: 51
Zusammenfassung: 
Chloroform/methanol was applied to cytoplasmic membranes of the thermophilic methanogens Methanothermobacter thermoautotrophicus and Methanothermobacter marburgensis as well as to the mesophile Methanosarcina mazei Gol. In any case, the chloroform/methanol extraction yielded only two proteins, subunit D (MtrD) of the Na+-translocating methylterrahydromethanopterin:coenzyme M methyltransferase and the proteolipid of the A(1)A(0) ATPase. Both polypeptides are assumed to be directly involved in ion translocation in their respective enzymes. but have not been studied in derail due to lack of simple isolation procedures. The rapid and selective isolation by chloroform/methanol offers a new way to obtain the large quantities of material required for biochemical analyses. As a first result, molecular and biochemical data suggest that the proteolipid from M. thermoautotrophicus is a duplication of the 8-kDa proteolipid usually present in other archaea, but it retained the conserved glutamate involved in proton translocation in every copy. This is the first 16-kDa proteolipid found in archaea. (C) 2001 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.
ISSN: 03781097
DOI: 10.1111/j.1574-6968.2001.tb10496.x

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