11 0 0 0 OA 翻訳伸長ダイナミクスと新生鎖フォールディング
- 著者
- 田口 英樹 茶谷 悠平 丹羽 達也
- 出版者
- 一般社団法人 日本生物物理学会
- 雑誌
- 生物物理 (ISSN:05824052)
- 巻号頁・発行日
- vol.59, no.3, pp.137-140, 2019 (Released:2019-05-25)
- 参考文献数
- 19
- 被引用文献数
- 1
Proteins do not instantaneously finish the synthesis and folding into functioning products, but experience the nascent peptidyl-tRNAs, defined as “nascent chains”, during the translation. So far, nascent chains are regarded as transient intermediates during the protein synthesis. However, recent advances have revealed that nascent chains are directly involved in a variety of cellular processes including self-maturation and the quality control system of protein and mRNA. In this review, we summarize recent progress on noncanonical translation dynamics and co-translational folding.
10 0 0 0 OA 生物物理学の概念と展望
2 0 0 0 マルチファセット・プロテインズ:拡大し変容するタンパク質の世界
- 著者
- 田口 英樹
- 雑誌
- 学術変革領域研究(A)
- 巻号頁・発行日
- 2020-11-19
1 0 0 0 OA シャペロニンGroELの作用機構:ATPと基質タンパク質の役割
- 著者
- 田口 英樹
- 出版者
- 一般社団法人 日本生物物理学会
- 雑誌
- 生物物理 (ISSN:05824052)
- 巻号頁・発行日
- vol.46, no.3, pp.130-136, 2006 (Released:2006-05-25)
- 参考文献数
- 27
- 被引用文献数
- 1 1
The chaperonin GroEL is an essential molecular chaperone that assists protein folding in the cell. ATP-dependent conformational change of GroEL leads to the stable binding of cochaperonin GroES, forming a cage-shaped complex that accommodates a substrate protein to complete the folding. After the elucidation of the outline of the molecular mechanism over the last decade, now we are ready to answer the important questions; how GroEL encapsulate the substrate protein? How the substrate protein influences the functional cycle of GroEL? What is the role of ATP hydrolysis in the GroEL-assisted folding? Is the folding in the GroEL-ES cavity is same as that in the bulk solution? Here I review the recent progress on the GroEL study and discuss the essential role of chaperonin GroEL.