Characterization of multimetric variants of ubiquitin carboxyl-terminal hydrolase L1 in water by small-angle neutron scattering
- High Energy Accelerator Research Organization, 1-1 Oho, Tsukuba-shi, Ibaraki 305-0801 (Japan) and Department of Neurology, Juntendo University School of Medicine, 2-1-1 Hongo 113-8421, Tokyo (Japan)
- Department of Neurology, Juntendo University School of Medicine, 2-1-1 Hongo 113-8421, Tokyo (Japan)
- Department of Mechanical Intelligence Engineering, Graduate School of Engineering, Hokkaido University, Kita 13, Nishi 8, Kita-ku, Sapporo 060-8628 (Japan)
- RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198 (Japan)
- Japan Atomic Energy Research Institute, 2-4 Tokaimura-shirakata-shirane, Naka-gun, Ibaraki 319-1195 (Japan)
- Department of Degenerative Neurological Diseases, National Institute of Neuroscience, National Centre of Neurology and Psychiatry, 4-1-1 Ogawa Higashi, Kodaira, Tokyo 187-8502 (Japan)
Here, we illustrated that the morphological structures of ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1) variants and Parkinson's disease (PD) exhibit good pathological correlation by a small-angle neutron scattering (SANS). UCH-L1 is a neuro-specific multiple functional enzyme, deubiquitinating, ubiquityl ligase, and also involved in stabilization of mono-ubiquitin. To examine the relationship between multiple functions of UCH-L1 and the configuration of its variants [wild-type, I93M (linked to familial Parkinson's disease), and S18Y (linked to reduced risk of Parkinson's disease)], in this report, we proposed that these were all self-assembled dimers by an application of a rotating ellipsoidal model; the configurations of these dimers were quite different. The wild-type was a rotating ellipsoidal. The globular form of the monomeric component deformed by the I93M mutation. Conversely, the S18Y polymorphism promoted the globularity. Thus, the multiple functional balance is closely linked to the intermolecular interactions between the UCH-L1 monomer and the final dimeric configuration.
- OSTI ID:
- 20798751
- Journal Information:
- Biochemical and Biophysical Research Communications, Vol. 339, Issue 2; Other Information: DOI: 10.1016/j.bbrc.2005.11.066; PII: S0006-291X(05)02560-X; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
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