Skip Navigation


Journal of Biochemistry Advance Access originally published online on October 15, 2007
Journal of Biochemistry 2007 142(6):707-713; doi:10.1093/jb/mvm187
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
142/6/707    most recent
mvm187v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Yoshizawa, K.
Right arrow Articles by Yamashita, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yoshizawa, K.
Right arrow Articles by Yamashita, I.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 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,*

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

*To whom correspondence should be addressed. Tel: +81-743-72-6135, Fax: +81-743-72-6196, E-mail: ichiro{at}ms.naist.jp

Received September 3, 2007; Accepted September 14, 2007


  Abstract

The denaturation of recombinant horse L-chain apoferritin (rLF), which is composed of 24 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. The 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

Abbreviations: rLF, recombinant horse L-chain apoferritin; rHF, recombinant horse H-chain apoferritin; CD, circular dichroism


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
L. S. Vedula, G. Brannigan, N. J. Economou, J. Xi, M. A. Hall, R. Liu, M. J. Rossi, W. P. Dailey, K. C. Grasty, M. L. Klein, et al.
A Unitary Anesthetic Binding Site at High Resolution
J. Biol. Chem., September 4, 2009; 284(36): 24176 - 24184.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.