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J. Biochem, 1988, Vol. 104, No. 5 837-840
© 1988 Japanese Biochemical Society

research-article

Site-Specific Mutagenesis of the Human Interleukin-1ß Gene: The Role of Arginine Residue at the N-Terminal Region

Takashi Kamogashira1, Maki Sakaguchi, Yasukazu Ohmoto, Keiko Mizuno, Ryoji Shimizu, Kenji Nagamura, Satoru Nakai, Yoshihiro Masui and Yoshikatsu Hirai

Laboratories of Cellular Technology, Otsuka Pharmaceutical Co., Ltd., Tokushima Tokushima 771–01

2 To whom correspondence should be addressed

Using the expression system for site-specific mutagenesis in Escherichia coli, we have made deletion mutants at the N-terminal or C-terminal region of human interleukin-1ß (IL-lß) consisting of 153 amino acids. The truncated mutants showed that at least 147 amino acids (numbers 4–150) in IL-1ß are necessary for the exertion of biological activity. When we changed the arginine at the 4th position (Arg in IL-1ß to other specific amino acids, there was a marked difference in the relative extent of biological and receptor binding activities among the mutants. The order of the mutants was Arg4=Lys4>Gln4>Gly4=des-Arg4>Asp4 Our results demonstrate that the arginine residue at the 4th position in IL-1ß is important, but not essential, for IL-1ß to exhibit its biological and receptor binding activities, and the positive charge at this site plays a key role for IL-1ß to exert the activities.


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