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MeSH Review:

Halorhodospira halophila

Kyndt, J.A. et al., Sasaki, J. et al., Lieutaud, C. et al.

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Disease relevance of Halorhodospira halophila

By using a dual plasmid system, one expressing the PYP from Halorhodospira halophila and the other expressing a two-gene operon, consisting of tyrosine ammonia lyase and p-hydroxycinnamic acid ligase, we are able to present evidence that a functionally active holo-PYP can be synthesized in Escherichia coli [1].

High impact information on Halorhodospira halophila

Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier [2].
Light-activation of the PAS domain protein photoactive yellow protein (PYP) is believed to trigger a negative phototactic response in the phototropic bacterium Halorhodospira halophila [3].

References

Heterologous production of Halorhodospira halophila holo-photoactive yellow protein through tandem expression of the postulated biosynthetic genes. Kyndt, J.A., Vanrobaeys, F., Fitch, J.C., Devreese, B.V., Meyer, T.E., Cusanovich, M.A., Van Beeumen, J.J. Biochemistry (2003) [Pubmed]
Study of the high-potential iron sulfur protein in Halorhodospira halophila confirms that it is distinct from cytochrome c as electron carrier. Lieutaud, C., Alric, J., Bauzan, M., Nitschke, W., Schoepp-Cothenet, B. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
Light-induced unfolding of photoactive yellow protein mutant M100L. Sasaki, J., Kumauchi, M., Hamada, N., Oka, T., Tokunaga, F. Biochemistry (2002) [Pubmed]

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