Non-iron porphyrins cause tumbling to blue light by an Escherichia coli mutant defective in hemG.
Previously we showed that an Escherichia coli hemH mutant, defective in the ultimate step of heme synthesis, ferrochelatase, is somewhat better than 100-fold more sensitive than its wild-type parent in tumbling to blue light. Here we explore the effect of a hemG mutant, defective in the penultimate step, protoporphyrinogen oxidase. We found that a hemG mutant also is somewhat better than 100-fold more sensitive in tumbling to blue light compared to its wild-type parent. The amount of non-iron porphyrins accumulated in hemG or hemH mutants was more than 100-fold greater than in wild type. The nature of these accumulated porphyrins is described. When heme was present, as in the wild type, the non-iron (non-heme) porphyrins were maintained at a relatively low concentration and tumbling to blue light at an intensity effective for hemG or hemH did not occur. The function of tumbling to light is most likely to allow escape from the lethality of intense light.
Yang
H
H
Department of Biochemistry, College of Agricultural and Life Sciences, University of Wisconsin-Madison, 53706, USA.
Sasarman
A
A
Inokuchi
H
H
Adler
J
J
D004926:Escherichia coli / Q000502:physiology*; D029968:Escherichia coli Proteins; D006418:Heme / Q000502:physiology*; D008027:Light; D009068:Movement; D010088:Oxidoreductases / Q000502:physiology*; D044925:Oxidoreductases Acting on CH-CH Group Donors; D011166:Porphyrins / Q000502:physiology*; D050768:Protoporphyrinogen Oxidase
D029968:Escherichia coli Proteins; D011166:Porphyrins; D006418:Heme; D010088:Oxidoreductases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C493977:HemG protein, E coli; D050768:Protoporphyrinogen Oxidase