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J. Biochem, 2003, Vol. 133, No. 3 371-376
© 2003 Japanese Biochemical Society

BIOTECHNOLOGY

Characterization of Folding Pathways of the Type-1 and Type-2 Periplasmic Binding Proteins MglB and ArgT

Kenji Kashiwagi1,2, Kiyotaka Shiba+,2, Kaoru Fukami-Kobayashi4, Tetsuo Noda3,5, Ken Nishikawa4 and Hiroshi Noguchi1

1 School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526; 2 Department of Protein Engineering, and 3 Department of Cell Biology, Cancer Institute, Japanese Foundation for Cancer Research, 1-37-1 Kami-Ikebukuro, Toshima-ku, Tokyo 170-8455; 4 National Institute of Genetics, 1111 Yada, Mishima, Shizuoka 411-8540; 5 Department of Molecular Genetics, University of Tohoku School of Medicine, 2-1 Seiryo-cho, Aoba-ku, Sendai 980-8575

The family of periplasmic binding proteins (PBPs) is believed to have arisen from a common ancestor and to have differentiated into two types. At first approximation, both types of PBPs have the same fold pattern, reflecting their common origin. However, the connection between the main chains of a type 2 PBP is more complicated than a type 1 PBP’s. We have been interested in the possibility that such structural changes affect the folding of PBPs. In this study, we have characterized the folding pathways of MglB (a type 1 PBP) and ArgT (a type 2 PBP) by using urea gradient gel electrophoresis, fast protein size–exclusion liquid chromatography and hydrophobic dye ANS binding assay. We found a distinct difference in folding between these two proteins. The folding of MglB followed a simple two-state transition model, whereas the folding of ArgT was more complicated.

+ To whom correspondence should be addressed. Tel: +81-3-3918-0111, Fax: +81-3-5394-3903, E-mail: kshiba{at}jfcr.or.jp


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