The interchain disulfide cross-linking of tropomyosin alters its regulatory properties and interaction with actin filament

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• 作者：Alexander M. Matyushenko^a ; ^b ; Natalia V. Artemova^a ; Daniil V. Shchepkin^c ; Galina V. Kopylova^c ; Salavat R. Nabiev^c ; Larisa V. Nikitina^c ; Dmitrii I. Levitsky^a ; ^d ; Sergey Y. Bershitsky^c ; ^{s.bershitsky@iip.uran.ru}
• 关键词：Tropomyosin ; Disulfide cross-linking ; Actin ; Ca2+-regulation of muscle contraction ; In vitro motility assay
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2017
• 出版时间：8 January 2017
• 年：2017
• 卷：482
• 期：2
• 页码：305-309
• 全文大小：530 K
• 卷排序：482

文摘

Two chains of tropomyosin (Tpm) can be cross-linked by disulfide bond. Cross-linking decreases Tpm affinity for actin and stability of Tpm–actin complex. Cross-linking enhances sliding velocity of thin filaments in the motility assay. Cross-linking significantly increases bending stiffness of thin filaments. Results can explain the role of Tpm cross-linking in human heart diseases.