Characterization of an <i>Escherichia coli</i> Mutant Pleiotropically Altered in Membrane-Bound Oxidoreductase Activities
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- COX John C.
- Department of Biology, University of Houston
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- GOLDSCHMIDT Eugene P.
- Department of Biology, University of Houston
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- JR. Peter JURTSHUK
- Department of Biology, University of Houston
抄録
An Escherichia coli mutant pleiotropically altered in membrane-bound oxidoreductase activities was isolated following nitrosoguanidine treatment. Mutant R23 was able to grow on glucose, but was unable to grow on succinate or other oxidizable substrates as a sole energy source. Isolated membranes prepared from R23 failed to oxidize succinate and formate; while NADH was oxidized at a reduced rate by membranes. The mutant also exhibited markedly reduced cytochrome content, but normal DL-lactate PMS reductase and H+-translocating ATPase activities relative to the parent strain. Bacteriophage P1kc was used to transduce R23 to growth on glycerol, DL-lactate or succinate; regardless of the selection procedure, each of the 179 transductants had gained the ability to grow on all three substrates. The suc- mutation in R23 appeared to be responsible for the loss of growth on oxidizable substrates, altered membrane-bound oxidoreductase activities, resistance to neomycin, and reduced levels of cytochrome components. The suc- mutation was localized in the 6 to 6.5min region of the E. coli chromosome map utilizing episomal transfers.
収録刊行物
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- MICROBIOLOGY and IMMUNOLOGY
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MICROBIOLOGY and IMMUNOLOGY 34 (6), 485-496, 1990
Center For Academic Publications Japan
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詳細情報
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- CRID
- 1573105977918809088
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- NII論文ID
- 130003483679
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- ISSN
- 03855600
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- 本文言語コード
- en
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- データソース種別
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- CiNii Articles