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Volume 272, Number 11, Issue of March 14, 1997 pp. 7285-7289
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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A cDNA Encoding Fish Fibroblast Growth Factor-2, Which Lacks Alternative Translation Initiation

(Received for publication, January 2, 1996, and in revised form, October 3, 1996)

From the Central Research Laboratory, Nippon Suisan Kaisha Limited, 559-6 Kitanomachi, Hachioji, Tokyo 192, Japan

Here, we describe the isolation of a rainbow trout cDNA clone that contains the entire fibroblast growth factor-2 (FGF-2; basic FGF) coding region. Interestingly, the rainbow trout cDNA contains a translation stop codon just upstream of the primary initiating methionine codon and so cannot give rise to the longer forms of FGF-2 that are produced in mammals by alternative translation initiation at leucines farther upstream. Transfection of human FGF-2 cDNA into fish cells shows that fish cells can initiate protein synthesis at an upstream leucine CUG codon; surprisingly, however, synthesis is initiated only at the most 5 CUG and not at the two subsequent CUG codons or the methionine AUG codon also used in mammalian cells. Like other FGF-2 proteins, bacterially produced rainbow trout FGF-2 protein binds tightly to heparin-Sepharose and also promotes the proliferation of fibroblast cells. However, the protein differs from all others previously identified at amino acids 121-123, which are part of the proposed highly conserved receptor-binding domain. Comparisons of the efficacies of recombinant wild-type and mutant rainbow trout FGF-2 proteins demonstrate that these three amino acids are critical to the activity of FGF-2.

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