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Science 28 September 1990:
Vol. 249. no. 4976, pp. 1567 - 1570
DOI: 10.1126/science.1699274
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Articles
Science, Vol 249, Issue 4976, 1567-1570
Copyright © 1990 by American Association for the Advancement of Science
Recovery of mitogenic activity of a growth factor mutant with a nuclear translocation sequence
T Imamura,
K Engleka,
X Zhan,
Y Tokita,
R Forough,
D Roeder,
A Jackson,
JA Maier,
T Hla,
and
T Maciag
Laboratory of Molecular Biology, Jerome H. Holland Laboratory for the Biomedical Sciences, American Red Cross, Rockville, MD 20855.
Heparin-binding growth factor-1 (HBGF-1) is an angiogenic polypeptide mitogen for mesoderm- and neuroectoderm-derived cells in vitro and remains biologically active after truncation of the amino-terminal domain (HBGF-1 alpha) of the HBGF-1 beta precursor. Polymerase chain reaction mutagenesis and prokaryotic expression systems were used to prepare a mutant of HBGF-1 alpha lacking a putative nuclear translocation sequence (amino acid residues 21 to 27; HBGF-1U). Although HBGF-1U retains its ability to bind to heparin, HBGF-1U fails to induce DNA synthesis and cell proliferation at concentrations sufficient to induce intracellular receptor-mediated tyrosine phosphorylation and c-fos expression. Attachment of the nuclear translocation sequence from yeast histone 2B at the amino terminus of HBGF-1U yields a chimeric polypeptide (HBGF-1U2) with mitogenic activity in vitro and indicates that nuclear translocation is important for this biological response.
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