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The FASEB Journal, Vol 3, 1760-1764, Copyright © 1989 by The Federation of American Societies for Experimental Biology

RESEARCH COMMUNICATIONS

Avidin-like domain in an epidermal growth factor homolog from a sea urchin

LT Hunt and WC Barker
Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, Washington, DC 20007.

We have found that a protein from the purple sea urchin has a carboxyl- terminal domain with striking sequence similarity to chicken avidin and bacterial streptavidin. All our evidence supports the homology of these sequences. Tetramers of avidin and streptavidin bind biotin strongly; the biotin binding site involves two to four tryptophans and probably an adjacent lysine in each chain. The presence of four tryptophans at equivalent positions in the sea urchin protein domain suggests that it may also be able to bind biotin and inhibit cell growth, as do the two other proteins. Alternatively, this domain may have acquired a new role as part of a multidomain protein.


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Copyright © 1989 by The Federation of American Societies for Experimental Biology.