EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	In situ characterization of mitochondrial Hsp60-Hsp10 chaperone complex under folding stress.
ジャーナル・号・ページ	Sci Adv, Vol. 11, Issue 43, Page eadw6064, Year 2025
掲載日	2025年10月24日
著者	Mingyu Jung / Minjung Kim / Su Jin Ham / Jongkyeong Chung / Soung-Hun Roh /
PubMed 要旨	Mitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein- ...Mitochondrial proteostasis is critical for maintaining mitochondrial function, and its disruption induces mitochondrial unfolded protein response, which up-regulates chaperones to alleviate protein-folding stress. However, how these chaperones mitigate protein-folding stress remains unclear. Here, using correlated cryo-electron tomography, we show that folding stress triggers marked mitochondrial morphological changes, including the accumulation of amorphous protein aggregates and increased abundance and spatial clustering of the mitochondrial heat shock protein 60-heat shock protein 10 (mtHsp60-Hsp10) complex. Subtomogram analysis revealed the in situ architecture and conformational heterogeneity of mtHsp60-Hsp10 under stress, which retains its canonical double-ring structure while adopting distinct football, half-football, and bullet-like states. Notably, the mtHsp60-Hsp10 complex encapsulates unstructured substrates through conserved hydrophobic interactions. We further demonstrate that knockdown of the mtHsp60-Hsp10 complex exacerbates folding stress, as evidenced by elevated cellular stress responses and activation of mitophagy. Our study defines the in situ structural properties of the mtHsp60-Hsp10 complex and provides mechanistic insight into how it safeguards mitochondrial proteostasis under folding stress.
リンク	Sci Adv / PubMed:41124257 / PubMed Central
手法	EM (サブトモグラム平均)
解像度	7.3 - 27.0 Å
構造データ	62702 9l8p EMDB-62702: mthsp60-hsp10_consensus PDB-9l8p: in situ structure of mtHsp60-Hsp10 手法: EM (サブトモグラム平均) / 解像度: 7.3 Å EMDB-62703: mthsp60-hsp10_without_symmetry 手法: EM (サブトモグラム平均) / 解像度: 8.1 Å EMDB-62704: mthsp60-hsp10_with_additional_interaction 手法: EM (サブトモグラム平均) / 解像度: 9.8 Å EMDB-62711: mthsp60-hsp10 with sparse substrate density 手法: EM (サブトモグラム平均) / 解像度: 8.5 Å EMDB-62713: mthsp60-hsp10 with bulky substrate density on single chamber 手法: EM (サブトモグラム平均) / 解像度: 8.7 Å EMDB-62714: mthsp60-hsp10 with bulky substrate density in both chamber 手法: EM (サブトモグラム平均) / 解像度: 8.5 Å EMDB-62747: mthsp60-hsp10 with U-shaped substrate density 手法: EM (サブトモグラム平均) / 解像度: 9.3 Å EMDB-65492: In situ structure of mtHsp60-Hsp10 bullet-like conformation 手法: EM (サブトモグラム平均) / 解像度: 21.0 Å EMDB-65493: in situ structure of mtHsp60-Hsp10 half-football conformation 手法: EM (サブトモグラム平均) / 解像度: 27.0 Å
化合物	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP / ATP, エネルギー貯蔵分子YM ChemComp-K*: Unknown entry / カリウムカチオン
由来	homo sapiens (ヒト)
キーワード	CHAPERONE / mtHsp60-Hsp10