AI Article Synopsis
- The hemG gene in E. coli K12 plays a key role in producing protoporphyrin IX, an important compound for heme and chlorophyll synthesis.
- The gene was identified through a mini-Mu cloning technique and can restore normal growth and enzyme activity in hemG mutant strains.
- The hemG gene consists of 546 nucleotides encoding a protein with a molecular mass of approximately 21,202 Da, marking it as the first gene cloned related to protoporphyrinogen oxidase activity in this bacterium.
Article Abstract
The hemG gene of Escherichia coli K12 is involved in the activity of protoporphyrinogen oxidase, the enzyme responsible for the conversion of protoporphyrinogen IX into protoporphyrin IX during heme and chlorophyll biosynthesis. The gene is located at min 87 on the genetic map of E. coli K12. The hemG gene was isolated by a mini-Mu in vivo cloning procedure. As expected, the hemG gene is able to restore normal growth to the hemG mutant, and the transformed cells display strong protoporphyrinogen oxidase activity. Sequencing of the hemG gene allowed us to identify an open reading frame of 546 nucleotides (181 amino acids), within the minimal fragment able to complement the mutant. The presumed molecular mass of the HemG protein is 21,202 Da, in agreement with values found by SDS-PAGE, in a DNA-directed coupled transcription-translation system. The identity of the first 18 amino acids at the amino-terminal end of the protein was confirmed by microsequencing. To our knowledge, this is the first cloning of a gene involved in the protoporphyrinogen oxidase activity of E. coli.
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| http://dx.doi.org/10.1139/m93-174 | DOI Listing |
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