Biochemical evidence for the reversed polarity of the outer membrane of the bacterial forespore.
Measurement of certain membrane-bound enzymic activities was used to study the orientation of the outer membrane of the double-membraned forespore of Bacillus megaterium KM. 2. Adenosine triphosphatase, NADH dehydrogenase and L-malate intact protoplasts, but were readily detected in intact stage II or IV forespores, consistent with reversed polarity of the outer forespore membrane relative to the mother-cell plasma membrane. 3. Measurement of NADH oxidase activity revealed that intact stage III forespores had the same high affinity for NADH as protoplast membrane preparations and protoplast lystates, consistent with ready access of NADH to oxidation sites on the outer forespores membrane. 4. Forespores and protoplasts showed osmometric behaviour in solutions of non-permanent solutes consistent with the presence of an intact permeability barrier in these structures.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D001410:Bacillus megaterium; D002462:Cell Membrane / Q000201:enzymology* / Q000378:metabolism; D002463:Cell Membrane Permeability; D008291:Malate Dehydrogenase / Q000378:metabolism; D009994:Osmolar Concentration; D010101:Oxygen Consumption; D011523:Protoplasts / Q000378:metabolism; D011808:Quinone Reductases; D013171:Spores, Bacterial / Q000201:enzymology* / Q000254:growth & development
D008291:Malate Dehydrogenase; D011808:Quinone Reductases; D000251:Adenosine Triphosphatases