2001
DOI: 10.1083/jcb.153.6.1151
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Tom40, the Pore-Forming Component of the Protein-Conducting Tom Channel in the Outer Membrane of Mitochondria

Abstract: Tom40 is the main component of the preprotein translocase of the outer membrane of mitochondria (TOM complex). We have isolated Tom40 of Neurospora crassa by removing the receptor Tom22 and the small Tom components Tom6 and Tom7 from the purified TOM core complex. Tom40 is organized in a high molecular mass complex of ∼350 kD. It forms a high conductance channel. Mitochondrial presequence peptides interact specifically with Tom40 reconstituted into planar lipid membranes and decrease the ion flow through the p… Show more

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Cited by 162 publications
(155 citation statements)
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“…Second derivative ATR FTIR spectra do not provide quantitative information for protein secondary structure, therefore, quantitative information was obtained by deconvolution of the FTIR spectra into Voigt‐shaped peaks. The peak area of individual amide I bands is correlated with secondary structure composition 41, 42, 43. The FTIR spectra were fitted with peaks centered at 1632 ± 3 cm −1 (β‐sheet), 1642 ± 3 cm −1 (random coil), 1657 ± 3 cm −1 (α‐helix), 1678 ± 4 cm −1 (β‐turn), and 1695 ± 4 cm −1 (β‐sheet).…”
Section: Resultsmentioning
confidence: 99%
“…Second derivative ATR FTIR spectra do not provide quantitative information for protein secondary structure, therefore, quantitative information was obtained by deconvolution of the FTIR spectra into Voigt‐shaped peaks. The peak area of individual amide I bands is correlated with secondary structure composition 41, 42, 43. The FTIR spectra were fitted with peaks centered at 1632 ± 3 cm −1 (β‐sheet), 1642 ± 3 cm −1 (random coil), 1657 ± 3 cm −1 (α‐helix), 1678 ± 4 cm −1 (β‐turn), and 1695 ± 4 cm −1 (β‐sheet).…”
Section: Resultsmentioning
confidence: 99%
“…Given that the TOM complex contains approximately eight Tom40 molecules, one pore might be formed by two Tom40 dimers (50). However, electron microscopy of puri ed Tom40 revealed particles mainly with one pore con rming that Tom40 forms the protein-conducting channel in an oligomeric assembly (45). The apparent diameter of the pores was determined to »2.5 nm, which is large enough to accommodate an unfolded or largely unfolded polypeptide chain as preproteins can traverse the outer membrane only in a mainly unfolded conformation (19, 44-46, 49, 51, 52).…”
Section: Translocation Across the Outer Membranementioning
confidence: 99%
“…Tom40 was isolated also from Neurospora crassa mitochondria. Reconstitution of these puri ed Tom40 molecules into liposomes showed that Tom40 alone is able to form a cationselective high-conductance channel, which is voltage-gated and binds mitochondrial presequences in a speci c manner (44)(45)(46)(47).…”
Section: Translocation Across the Outer Membranementioning
confidence: 99%
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