Multiple functions of tail‐anchor domains of mitochondrial outer membrane proteins

Habib, Shukry J.; Vasiljev, Andreja; Neupert, Walter; Rapaport, Doron

doi:10.1016/s0014-5793(03)01325-5

Cited by 40 publications

(42 citation statements)

References 26 publications

(43 reference statements)

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“…A receptor-like function of Tom5 would be expected to reside in its cytosolic domain. However, a fusion protein consisting of the transmembrane region of yeast Tom5 with the unrelated protein Fis1 replacing the cytosolic domain is sufficient to rescue the growth phenotype and the mitochondrial protein import defect of the yeast Tom5 deletion mutant (24,33). This makes a receptor-like function of Tom5 unlikely.…”

Section: Discussionmentioning

confidence: 99%

“…Protein import into S. cerevisiae mitochondria deficient in Tom5 rescued by Fis1-Tom5C. Mitochondria were isolated from S. cerevisiae tom5⌬ cells, tom5⌬ cells expressing a fusion protein consisting of the amino-terminal domain of Fis1 and the transmembrane region of Tom5 (24), and wild-type (wt) cells. Protein import reactions were performed as described in Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Mitochondria used for protein import studies were isolated from the N. crassa wild-type strain 74A, the N. crassa tom5 RIP mutant strain, the S. cerevisiae wild-type strain YPH499, the S. cerevisiae tom5⌬ mutant strain (a kind gift from Dr. N. Pfanner, University of Freiburg, Freiburg, Germany) and the S. cerevisiae tom5⌬ strain rescued by a plasmid carrying the sequence information for a Fis1-Tom5C fusion protein (24).…”

Section: Strains and Growthmentioning

confidence: 99%

“…As a model protein we used the chimeric protein Fis1-Tom5C (24). Protein import studies were performed using (24).…”

Section: Depletion Of Tom5 In Neurospora Has No Effect On Import Of Mmentioning

confidence: 99%

“…As a model protein we used the chimeric protein Fis1-Tom5C (24). Protein import studies were performed using (24). Isolated mitochondria were solubilized in digitonin at 37°C, subjected to BN-PAGE, blotted to PVDF membrane, and immunodecorated with an antibody against Tom40.…”

Section: Depletion Of Tom5 In Neurospora Has No Effect On Import Of Mmentioning

confidence: 99%

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Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria

Schmitt

Ahting²,

Eichacker

et al. 2005

Journal of Biological Chemistry

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Transport of nuclear encoded proteins into mitochondria is mediated by multisubunit translocation machineries in the outer and inner membranes of mitochondria. The TOM complex contains receptor and pore components that facilitate the recognition of preproteins and their transfer through the outer membrane. In addition, the complex contains a set of small proteins. Tom7 and Tom6 have been found in Neurospora and yeast, Tom5 has been found so far only in the latter organism. In the present study, we identified Neurospora Tom5 and analyzed its function in comparison to yeast Tom5, which has been proposed to play a role as a receptor-like component. Neurospora Tom5 crosses the outer membrane with its carboxyl terminus facing the intermembrane space like the other small Tom components. The temperature-sensitive growth phenotype of the yeast TOM5 deletion was rescued by overexpression of Neurospora Tom5. On the other hand, Neurospora cells deficient in tom5 did not exhibit any defect in growth. The structural stability of TOM complexes from cells devoid of Tom5 was significantly altered in yeast but not in Neurospora. The efficiency of protein import in Neurospora mitochondria was not affected by deletion of tom5, whereas in yeast it was reduced as compared with wild type. We conclude that the main role of Tom5, rather than being a receptor, is maintaining the structural integrity of the TOM complex.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Strains and Growthmentioning

confidence: 99%

“…As a model protein we used the chimeric protein Fis1-Tom5C (24). Protein import studies were performed using (24).…”

Section: Depletion Of Tom5 In Neurospora Has No Effect On Import Of Mmentioning

confidence: 99%

Section: Depletion Of Tom5 In Neurospora Has No Effect On Import Of Mmentioning

confidence: 99%

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Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria

Schmitt

Ahting²,

Eichacker

et al. 2005

Journal of Biological Chemistry

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Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

2021

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The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.

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Membrane Insertion of Tail‐anchored Proteins

Schuldiner

Schwappach

Weissman

2010

Encyclopedia of Life Sciences

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Tail‐anchored (TA) proteins are a special class of transmembrane proteins, which harbour only a single hydrophobic segment adjacent to their most C ‐terminus. This anchor must be inserted into membranes posttranslationally to allow for their correct cellular localization. Although TA proteins have essential cellular roles such as signal transduction, apoptosis and vesicle fusion, their biogenesis route has for many years remained unknown. Recently, several advances have created a new understanding of the TA protein insertion machinery. Uncovering the machinery responsible for the biogenesis of TA proteins should further our ability to understand a wide variety of diseases such as forms of cancer caused by activation of the TA protein oncogene BCL2 . Key concepts: Tail‐anchored proteins have C ‐terminal hydrophobic domains. Tail‐anchored proteins are inserted posttranslationally into the membrane. The GET complex inserts tail‐anchored proteins into the endoplasmic reticulum membrane in yeast. The TRC complex chaperones tail‐anchored proteins into membranes in humans.

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Multiple functions of tail‐anchor domains of mitochondrial outer membrane proteins

Cited by 40 publications

References 26 publications

Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria

Role of Tom5 in Maintaining the Structural Stability of the TOM Complex of Mitochondria

Evolutionarily conserved mechanism for membrane recognition from bacteria to mitochondria

Membrane Insertion of Tail‐anchored Proteins

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