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Effects of cataract-causing mutations W59C and W151C on ßB2-crystallin structure, stability and folding.
Zhao, Wei-Jie; Xu, Jia; Chen, Xiang-Jun; Liu, Hui-Hui; Yao, Ke; Yan, Yong-Bin.
Afiliación
  • Zhao WJ; State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
  • Xu J; Eye Center of the 2nd Affiliated Hospital, Medical College of Zhejiang University, Hangzhou 310009, China.
  • Chen XJ; State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
  • Liu HH; State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China.
  • Yao K; Eye Center of the 2nd Affiliated Hospital, Medical College of Zhejiang University, Hangzhou 310009, China. Electronic address: xlren@zju.edu.cn.
  • Yan YB; State Key Laboratory of Membrane Biology, School of Life Sciences, Tsinghua University, Beijing 100084, China. Electronic address: ybyan@tsinghua.edu.cn.
Int J Biol Macromol ; 103: 764-770, 2017 Oct.
Article en En | MEDLINE | ID: mdl-28528950
ß/γ-Crystallins, the predominant structural proteins in vertebrate lens with lifelong stability to maintain lens transparency, share a high similarity in their primary sequences and tertiary structures. Four conserved Trp residues have been shown to be important to γ-crystallin structure, stability and protection against UV irradiation, whereas their roles in ß-crystallins remain elusive. Herein we found that two congenital cataract-causing mutations, W59C and W151C, dramatically decreased ßB2-crystallin solubility and stability against thermal and guanidine hydrochloride-induced denaturation. The two mutated proteins were prone to form aggregates when irradiated by UV light in the tubes or exogenously expressed in the cells. Although W59 and W151 are structurally identical in ß/γ-crystallin domains, substituting them by Cys led to dissimilar influences on ßB2-crystallin stability. Our results suggested that the conserved Trp residues might play a more crucial role in the correct folding and structural integrity of ß-crystallin domains than in γ-crystallins.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catarata / Pliegue de Proteína / Cadena B de beta-Cristalina / Mutación Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2017 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Catarata / Pliegue de Proteína / Cadena B de beta-Cristalina / Mutación Límite: Humans Idioma: En Revista: Int J Biol Macromol Año: 2017 Tipo del documento: Article País de afiliación: China Pais de publicación: Países Bajos