Jun, 2004
Insertional-fusion of basic fibroblast growth factor endowed ribonuclease 1 with enhanced cytotoxicity by steric blockade of inhibitor interaction
FEBS LETTERS
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- Volume
- 568
- Number
- 1-3
- First page
- 39
- Last page
- 43
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1016/j.febslet.2004.05.007
- Publisher
- ELSEVIER SCIENCE BV
Basic fibroblast growth factor (bFGF) was inserted in the middle of human ribonuclease 1 (RNase1) sequence at an RNase inhibitor (RI)-binding site (Gly89) by a new gene fusion technique, insertional-fusion. The resultant insertional-fusion protein (CL-RFN89) was active both as bFGF and as RNase. Furthermore, it acquired an additional ability of evading RI through steric blockade of RI-binding caused by fused bFGF domain. As a result, CL-RFN89 showed stronger growth inhibition on B16/BL6 melanoma cells than an RI-sensitive tandem fusion protein. Thus, the insertional-fusion technique increases accessible positions for gene fusion on RNase, resulting in construction of a potent cytotoxic RNase. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
- Link information
- ID information
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- DOI : 10.1016/j.febslet.2004.05.007
- ISSN : 0014-5793
- Web of Science ID : WOS:000222205200009