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. 1986 Nov;168(2):631–635. doi: 10.1128/jb.168.2.631-635.1986

Purification of the phoU protein, a negative regulator of the pho regulon of Escherichia coli K-12.

B P Surin, N E Dixon, H Rosenberg
PMCID: PMC213527  PMID: 3536855

Abstract

Thermally induced transcription of the phoU gene under control of the major leftward promoter, pL, of phage lambda resulted in production of the PhoU protein to compose approximately 5% of the total cell protein. The PhoU protein was present in the cytoplasm in the form of an aggregate. The amino acid composition and N-terminal amino acid sequence of the purified protein confirmed the reading frame established earlier for the phoU gene.

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Selected References

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