ArticleMolecular and cellular biology2000
Mitochondrial protein import motor: the ATPase domain of matrix Hsp70 is crucial for binding to Tim44, while the peptide binding domain and the carboxy-terminal segment play a stimulatory role.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 66 citations in OpenAlex.
- Therapeutic targets in diabetic peripheral neuropathy: heat shock proteins.Frontiers in endocrinology · 2025Review
- Alternative ATPase domain interactions in eukaryotic Hsp70 chaperones.Frontiers in molecular biosciences · 2023Review
- Mapping protein interactions in the active TOM-TIM23 supercomplex.Nature communications · 2021Article
- Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response.Open biology · 2020Review
- Identification of small RNAs during cold acclimation in Arabidopsis thaliana.BMC plant biology · 2020Article
- Structure and Molecular Mechanism of ER Stress Signaling by the Unfolded Protein Response Signal Activator IRE1.Frontiers in molecular biosciences · 2019Review
- Hsp70 at the membrane: driving protein translocation.BMC biology · 2018Review
- Article
- Promoting Neuronal Tolerance of Diabetic Stress: Modulating Molecular Chaperones.International review of neurobiology · 2016Review
- Architecture of the TIM23 inner mitochondrial translocon and interactions with the matrix import motor.The Journal of biological chemistry · 2014Article
- Inducible HSP70 regulates superoxide dismutase-2 and mitochondrial oxidative stress in the endothelial cells from developing lungs.American journal of physiology. Lung cellular and molecular physiology · 2014Article
- Overexpression of mitochondrial Hsp70/Hsp75 protects astrocytes against ischemic injury in vitro.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2008Article
- Novel germline variants identified in the inner mitochondrial membrane transporter TIMM44 and their role in predisposition to oncocytic thyroid carcinomas.British journal of cancer · 2006Article
- Preliminary crystallographic studies of yeast mitochondrial peripheral membrane protein Tim44p.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells.Molecular and cellular biochemistry · 2005Article
- 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
- Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria.The EMBO journal · 2003Article
- An Hsp70 family chaperone, mortalin/mthsp70/PBP74/Grp75: what, when, and where?Cell stress & chaperones · 2002Review
- The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.The EMBO journal · 2002Article
- Protein unfolding by mitochondria. The Hsp70 import motor.EMBO reports · 2000Review
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The import motor for preproteins that are targeted into the mitochondrial matrix consists of the matrix heat shock protein Hsp70 (mtHsp70) and the translocase subunit Tim44 of the inner membrane. mtHsp70 interacts with Tim44 in an ATP-dependent reaction cycle, binds to preproteins in transit, and drives their translocation into the matrix. While different functional mechanisms are discussed for the mtHsp70-Tim44 machinery, little is known about the actual mode of interaction of both proteins. Here, we have addressed which of the three Hsp70 regions, the ATPase domain, the peptide binding domain, or the carboxy-terminal segment, are required for the interaction with Tim44. By two independent means, a two-hybrid system and coprecipitation of mtHsp70 constructs imported into mitochondria, we show that the ATPase domain interacts with Tim44, although with a reduced efficiency compared to the full-length mtHsp70. The interaction of the ATPase domain with Tim44 is ATP sensitive. The peptide binding domain and carboxy-terminal segment are unable to bind to Tim44 in the absence of the ATPase domain, but both regions enhance the interaction with Tim44 in the presence of the ATPase domain. We conclude that the ATPase domain of mtHsp70 is essential for and directly interacts with Tim44, clearly separating the mtHsp70-Tim44 interaction from the mtHsp70-substrate interaction.
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