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Characterization of bromoethanesulfonate-resistant mutants of methanococcus voltae: evidence of a coenzyme M transport system

Journal Article · · J. Bacteriol.; (United States)
OSTI ID:6470046
Mutants of Methanococcus voltae were isolated that were resistant to the coenzyme M (CoM; 2-mercaptoethanesulfonic acid) analog 2-bromoethanesulfonic acid (BES). The mutants displayed a reduced ability accumulate (/sup 35/S)BES relative to the sensitive parental strain. BES inhibited methane production from CH/sub 3/-S-CoM in cell extracts prepared from wild-type sensitive or resistant strains. BES uptake required the presence of both CO/sub 2/ and H/sub 2/ and was inhibited by N-ethylmaleimide and several reagents that are known to disrupt energy metabolism. The mutants showed normal uptake of isoleucine and were not cross-resistant to either azaserine or 5-methyltrypotophan and, thus, were neither defective in general energy-dependent substrate transport nor envelope permeability. Both HS-CoM and CH/sub 3/-S-CoM prevented the uptake of BES and protected cells from inhibition by it. The authors propose that M. voltae has an energy-dependent, carrier-mediated uptake system for HS-CoM and CH/sub 3/-S-CoM which can also mediate uptake of BES.
Research Organization:
Univ. of Illinois, Urbana
DOE Contract Number:
FG02-84ER13241
OSTI ID:
6470046
Journal Information:
J. Bacteriol.; (United States), Journal Name: J. Bacteriol.; (United States) Vol. 169:2; ISSN JOBAA
Country of Publication:
United States
Language:
English