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J. Biochem, 2003, Vol. 133, No. 6 731-736
© 2003 Japanese Biochemical Society

CELL

Conformational Dynamics of ß2-Microglobulin Analyzed by Reduction and Reoxidation of the Disulfide Bond

Masayo Gozu1, Young Ho Lee1, Yumiko Ohhashi1, Masaru Hoshino1, Hironobu Naiki2 and Yuji Goto1,+

1 Institute for Protein Research, Osaka University and CREST, Japan Science and Technology Cooperation, 3-2 Yamadaoka, Suita, Osaka 565-0871; 2 Department of Pathology, Fukui Medical University, and CREST, Japan Science and Technology Cooperation, Matsuoka, Fukui 910-1193

Although native ß2-microglobulin (ß2-m), the light chain of the major histocompatibility complex class I antigen, assumes an immunoglobulin domain fold, it is also found as a major component of dialysis-related amyloid fibrils. In the amyloid fibrils, the conformation of ß2-m is considered to be largely different from that of the native state, and a monomeric denatured form is likely to be a precursor to the amyloid fibril. To obtain insight into the conformational dynamics of ß2-m leading to the formation of amyloid fibrils, we studied the reduction and reoxidation of the disulfide bond by reduced and oxidized dithiothreitol, respectively, and the effects on the reduction of the chaperonin GroEL, a model protein that might destabilize the native state of ß2-m. We show that ß2-m occasionally unfolds into a denatured form even under physiological conditions and that this transition is promoted upon interaction with GroEL. The results imply that in vivo interactions of ß2-m with other proteins or membrane components could destabilize its native structure, thus stabilizing the amyloid precursor.

+ To whom correspondence should be addressed. Fax: +81-6-6879-8614, E-mail: ygoto{at}protein.osaka-u.ac.jp


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