ArticleThe EMBO journal1996
Differential requirement for the mitochondrial Hsp70-Tim44 complex in unfolding and translocation of preproteins.
Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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Who cites it
32 citing papers in PubMed, 117 citations in OpenAlex.
- LETMD1 regulates mitochondrial protein synthesis and import to guard brown fat mitochondrial integrity and function.iScience · 2024Article
- 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
- TIMM44 is a potential therapeutic target of human glioma.Theranostics · 2022Article
- A Synthetic Biology Workflow Reveals Variation in Processing and Solubility of Nitrogenase Proteins Targeted to Plant Mitochondria, and Differing Tolerance of Targeting Sequences in a Bacterial Nitrogenase Assay.Frontiers in plant science · 2020Article
- Abnormal Mitochondrial Quality Control in Neurodegenerative Diseases.Frontiers in cellular neuroscience · 2020Review
- DNA Polymerase Beta Participates in Mitochondrial DNA Repair.Molecular and cellular biology · 2017Article
- Mitochondrial quality control in amyotrophic lateral sclerosis: towards a common pathway?Neural regeneration research · 2017Review
- Mutations in the Yeast Hsp70, Ssa1, at P417 Alter ATP Cycling, Interdomain Coupling, and Specific Chaperone Functions.Journal of molecular biology · 2015Article
- Role of membrane contact sites in protein import into mitochondria.Protein science : a publication of the Protein Society · 2015Review
- Role of the loop L4,5 in allosteric regulation in mtHsp70s: in vivo significance of domain communication and its implications in protein translocation.Molecular biology of the cell · 2014Article
- Distinct forms of mitochondrial TOM-TIM supercomplexes define signal-dependent states of preprotein sorting.Molecular and cellular biology · 2010Article
- Residues of Tim44 involved in both association with the translocon of the inner mitochondrial membrane and regulation of mitochondrial Hsp70 tethering.Molecular and cellular biology · 2008Article
- A cooperative action of the ATP-dependent import motor complex and the inner membrane potential drives mitochondrial preprotein import.Molecular and cellular biology · 2007Article
- On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.Cell stress & chaperones · 2006Review
- The protein import motor of mitochondria: a targeted molecular ratchet driving unfolding and translocation.The EMBO journal · 2002Article
- The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.The EMBO journal · 2002Article
- Surface accessibility of the 70-kilodalton Chlamydia trachomatis heat shock protein following reduction of outer membrane protein disulfide bonds.Infection and immunity · 2002Article
- Mitochondrial import driving forces: enhanced trapping by matrix Hsp70 stimulates translocation and reduces the membrane potential dependence of loosely folded preproteins.Molecular and cellular biology · 2001Article
- The mitochondrial Hsp70-dependent import system actively unfolds preproteins and shortens the lag phase of translocation.The EMBO journal · 2001Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial heat shock protein Hsp70 is essential for import of nuclear-encoded proteins, involved in both unfolding and membrane translocation of preproteins. mtHsp70 interacts reversibly with Tim44 of the mitochondrial inner membrane, yet the role of this interaction is unknown. We analysed this role by using two yeast mutants of mtHsp70 that differentially influenced its interaction with Tim44. One mutant mtHsp70 (Ssc1-2p) efficiently bound preproteins, but did not show a detectable complex formation with Tim44; the mitochondria imported loosely folded preproteins with wild-type kinetics, yet were impaired in unfolding of preproteins. The other mutant Hsp70 (Ssc1-3p') bound both Tim44 and preproteins, but the mitochondria did not import folded polypeptides and were impaired in import of unfolded preproteins; Ssc1-3p' was defective in its ATPase domain and did not undergo a nucleotide-dependent conformational change, resulting in permanent binding to Tim44. The following conclusions are suggested. (i) The import of loosely folded polypeptides (translocase function of mtHsp70) does not depend on formation of a detectable Hsp70-Tim44 complex. Two explanations are possible: a trapping mechanism by soluble mtHsp70, or a weak/very transient interaction of Ssc1-2p with Tim44 that leads to a weak force generation sufficient for import of loosely folded, but not folded, polypeptides. (ii) Import of folded preproteins (unfoldase function of mtHsp70) involves a reversible nucleotide-dependent interaction of mtHsp70 with Tim44, including a conformational change in mtHsp70. This is consistent with a model that the dynamic interaction of mtHsp70 with Tim44 generates a pulling force on preproteins which supports unfolding during translocation.
Indexed as
Identifiers
8654364PMC450202W1591848571What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.