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Journal of Biochemistry Advance Access published online on October 15, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm187
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© 2007 The Japanese Biochemical Society

Effect of N-terminal residues on the structural stability of recombinant horse L-chain apoferritin in an acidic environment

Keiko Yoshizawa1,2, Yumiko Mishima1,2, Sam-Yong Park3, Jonathan G. Heddle1,3, Jeremy R. H. Tame3, Kenji Iwahori1,2, Mime Kobayashi1,2 and Ichiro Yamashita1,2

1 CREST, Japan Science and Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama, 332-0012, Japan
2 Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan
3 Protein Design Laboratory, Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan

Correspondence should be addressed to: Professor Ichiro Yamashita, Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. E-mail: ichiro{at}ms.naist.jp, Phone: +81-743-72-6135, FAX: +81-743-72-6196

Received September 3, 2007; Accepted September 14, 2007


  Abstract

The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of twenty-four L-chain subunits, in acidic solution was studied. Using two rLF mutants lacking four (Fer4) or eight (Fer8) N-terminal amino acid residues, the effect of N-terminal residues on the protein's stability was investigated. Of the two mutants and wild-type rLF, the tertiary and secondary structures of Fer8 were found to be most sensitive to an acidic environment. Fer8 protein dissociated easily into subunit dimers at or below pH 2.0. Comparing the crystal structures of the mutant proteins, deletion of the N-terminal residues was found to result in fewer inter- and intra-subunit hydrogen bonds. The loss of these bonds is assumed to be responsible for lower endurance against acidic denaturation in N-terminus-deleted mutants. These results indicated that the inter- and intra-subunit hydrogen bonds of N-terminal residues affect the denaturation, especially oligomer formation of apoferritin subunits and will be of use in designing ferritin-based nanodevices.

Key Words: acidic denaturation, apoferritin, ferritin, hydrogen bond, protein structure


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