ArticleThe Journal of cell biology1999
The J-related segment of tim44 is essential for cell viability: a mutant Tim44 remains in the mitochondrial import site, but inefficiently recruits mtHsp70 and impairs protein translocation.
Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 50 citations in OpenAlex.
- ALS/FTD mutations in UBQLN2 are linked to mitochondrial dysfunction through loss-of-function in mitochondrial protein import.Human molecular genetics · 2021Article
- The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.3 Biotech · 2015Article
- Probing the Biology of Giardia intestinalis Mitosomes Using In Vivo Enzymatic Tagging.Molecular and cellular biology · 2015Article
- Genetic analysis of complex interactions among components of the mitochondrial import motor and translocon in Saccharomyces cerevisiae.Genetics · 2012Article
- Direct interaction of mitochondrial targeting presequences with purified components of the TIM23 protein complex.The Journal of biological chemistry · 2011Article
- Complexity of Hsp90 in organelle targeting.Plant molecular biology · 2008Article
- 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
- 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
- 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
- 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.Molecular and cellular biology · 2000Article
- An N-terminal region of mot-2 binds to p53 in vitro.Neoplasia (New York, N.Y.)Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tim44 is a protein of the mitochondrial inner membrane and serves as an adaptor protein for mtHsp70 that drives the import of preproteins in an ATP-dependent manner. In this study we have modified the interaction of Tim44 with mtHsp70 and characterized the consequences for protein translocation. By deletion of an 18-residue segment of Tim44 with limited similarity to J-proteins, the binding of Tim44 to mtHsp70 was weakened. We found that in the yeast Saccharomyces cerevisiae the deletion of this segment is lethal. To investigate the role of the 18-residue segment, we expressed Tim44Delta18 in addition to the endogenous wild-type Tim44. Tim44Delta18 is correctly targeted to mitochondria and assembles in the inner membrane import site. The coexpression of Tim44Delta18 together with wild-type Tim44, however, does not stimulate protein import, but reduces its efficiency. In particular, the promotion of unfolding of preproteins during translocation is inhibited. mtHsp70 is still able to bind to Tim44Delta18 in an ATP-regulated manner, but the efficiency of interaction is reduced. These results suggest that the J-related segment of Tim44 is needed for productive interaction with mtHsp70. The efficient cooperation of mtHsp70 with Tim44 facilitates the translocation of loosely folded preproteins and plays a crucial role in the import of preproteins which contain a tightly folded domain.
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