ArticleThe EMBO journal2002
The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 52 citations in OpenAlex.
- Lon/Pim1-mediated degradation of presequence translocase-associated motor components Pam16 and Pam18 in Saccharomyces cerevisiae.The Biochemical journal · 2025Article
- A first-in-class TIMM44 blocker inhibits bladder cancer cell growth.Cell death & disease · 2024Article
- The mitochondrial protein TIMM44 is required for angiogenesis in vitro and in vivo.Cell death & disease · 2023Article
- Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones.Frontiers in molecular biosciences · 2023Review
- TIMM44 is a potential therapeutic target of human glioma.Theranostics · 2022Article
- Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.Open biology · 2020Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- A complex of Cox4 and mitochondrial Hsp70 plays an important role in the assembly of the cytochrome c oxidase.Molecular biology of the cell · 2013Article
- Abrogation of MMP-9 gene protects against the development of retinopathy in diabetic mice by preventing mitochondrial damage.Diabetes · 2011Article
- Primary sequence that determines the functional overlap between mitochondrial heat shock protein 70 Ssc1 and Ssc3 of Saccharomyces cerevisiae.The Journal of biological chemistry · 2011Article
- Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Lessons from the genome sequence of Neurospora crassa: tracing the path from genomic blueprint to multicellular organism.Microbiology and molecular biology reviews : MMBR · 2004Review
- J protein cochaperone of the mitochondrial inner membrane required for protein import into the mitochondrial matrix.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
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3 authors at 1 institution in 1 country.
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Abstract
Ssc1, a molecular chaperone of the Hsp70 family, drives preprotein import into the mitochondrial matrix by a specific interaction with the translocase component Tim44. Two other mitochondrial Hsp70s, Ssc3 (Ecm10) and Ssq1, show high sequence homology to Ssc1 but fail to replace Ssc1 in vivo, possibly due to their inability to interact with Tim44. We analyzed the structural basis of the Tim44 interaction by the construction of chimeric Hsp70 proteins. The ATPase domains of all three mitochondrial Hsp70s were shown to bind to Tim44, supporting the active motor model for the Hsp70 mechanism during preprotein translocation. The peptide-binding domain of Ssc1 sustained binding of Tim44, while the peptide-binding domains of Ssc3 and Ssq1 exerted a negative effect on the interaction of the ATPase domains with Tim44. A mutation in the peptide-binding domain of Ssc1 resulted in a similar negative effect not only on the ATPase domain of Ssc1, but also of Ssq1 and Ssc3. Hence, the determination of a crucial Hsp70 function via the peptide-binding domain suggests a new regulatory principle for Hsp70 domain cooperation.
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