Yeast Two-Hybrid Screening Identifies Binding Partners of Human Tom34 That Have ATPase Activity and Form a Complex with Tom34 in the Cytosol
Abstract
In the accompany paper (Mukhopadhyay, A., Avramova, L. V. and Weiner, H., Arch. Biochem. Biophys.), it was shown that Tom34, a previously proposed putative translocase of the mitochondrial outer membrane, binds to the mature region of a precursor protein and appears to be a cytosol protein. Here Tom34 was used as bait in a yeast two-hybrid screening to search for its potential binding partners. Two of the identified proteins were the ATPase-related valosin-containing protein (VCP) and the lysosomal H(+)-transporting ATPase member M (ATP6M). Tom34 was found primarily in the cytosol while VCP and ATP6M were found in the cytosol as well as in nonmitochondrial organelles. Tom34 formed a approximately 400-kDa complex with them in the cytosol. Tom34 was found to possess a weak ATPase activity that did not change when associated with VCP. The tetratricopeptide repeat (TPR) motif region of Tom34 (residue 201-256) was responsible for binding to the other proteins. Tom34 appears not to be a member of the mitochondrial outer membrane translocase family but might function as a chaperone-like protein during protein translocation.
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Tom34 is found predominantly in the cytosol and binds Hsp90 and Hsp70, as does Tom70.
“Although associated with mitochondria, Tom34 is found more predominantly in the cytosol and binds to the chaperone proteins Hsp90 and Hsp70, as does Tom70 (66–68).”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [66]
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Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works
- Authors
- Yang, C.-S., & Weiner, H.
- Affiliations
- Purdue University West Lafayette (US)
- Corresponding author
- Weiner, Henry
- Venue
- Archives of Biochemistry and Biophysics
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 400
- Issue
- 1
- Pages
- 105-110
- ISSN
- 0003-9861 (ISSN-L)
- OpenAlex
- W2098928068
- Cited by
- 16
- References
- 0
- Citations by year
- 2023: 1 · 2021: 1 · 2019: 1 · 2016: 1
- FWCI
- 0.35
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Archives of Biochemistry and Biophysics (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Purdue University
- National Institute on Alcohol Abuse and Alcoholism (AA 10795, R01AA010795)
- National Institute of General Medical Sciences (GM 53269, R01GM053269)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Keywords
- VCP, protein-protein interaction, ATPase activity, chaperone-like protein, protein translocation
- MeSH terms
- Mitochondrial Precursor Protein Import Complex Proteins, Adenosine Triphosphatases, Animals, Carrier Proteins, Cloning, Molecular, Cytosol, HeLa Cells, Humans, Hydrolysis, Isoelectric Focusing, Liver, Microscopy, Fluorescence, Mitochondria, Protein Binding, Recombinant Proteins, Subcellular Fractions, Electrophoresis, Gel, Two-Dimensional, Protein Structure, Tertiary, Two-Hybrid System Techniques, Protein Transport, Mitochondrial Membrane Transport Proteins, Rats
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