The subcellular distribution of the soluble flavohaemoglobin (HMP) of Escherichia coli has been determined. Cells over-expressing HMP from the cloned hmp gene on a multicopy plasmid were fractionated by osmotic shock and lysozyme treatment. Spectral analysis of subcellular fractions showed the CO-binding haemoprotein to be cytoplasmic. However, Western blotting using antibody raised to purified HMP revealed approximately 30% of the protein to be periplasmic in the over-expressing strain. Western analysis also revealed substantial levels of periplasmic HMP in a strain expressing only chromosomally encoded protein but none in an hmp mutant. The results are discussed in relation to protein function and the similar distribution reported for Vitreoscilla globin. © 1995.
Vasudevan, S. G., Tang, P., Dixon, N. E., & Poole, R. K. (1995). Distribution of the flavohaemoglobin, HMP, between periplasm and cytoplasm in Escherichia coli. FEMS Microbiology Letters, 125(2–3), 219–224. https://doi.org/10.1016/0378-1097(94)00501-H