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Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution.

Neuroglobin (Ngb) is a recently discovered vertebrate heme protein that can reversibly bind oxygen that is expressed in the brain. Zebrafish and human Ngb share about 50% amino acid sequence identity. These Ngb proteins consist of four compact protein structural unit "modules" referred to as M1-M4. In the present study, we investigated the effects of module substitution on the properties of Ngb. Specifically, we prepared and characterized a chimeric ZHZZ Ngb in which the heme-binding module M2 of zebrafish Ngb was replaced by the comparable human Ngb module. Our results showed that the chimeric ZHZZ was stable and formed almost the identical heme-environmental and alpha-helical structure as the human and zebrafish Ngb proteins, suggesting that the structure of Ngb has been evolutionarily conserved.[1]

References

  1. Preparation and characterization of a chimeric zebrafish-human neuroglobin engineered by module substitution. Wakasugi, K., Morishima, I. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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