Abstract
The F0F1-ATPase complex of yeast mitochondria contains three mitochondrial and at least 17 nuclear gene products. The coordinate assembly of mitochondrial and cytosolic translation products relies on chaperones and specific factors that stabilize the pools of some unassembled subunits. Atp10p was identified as a mitochondrial inner membrane component necessary for the biogenesis of the hydrophobic F0 sector of the ATPase. Here we show that, following its synthesis on mitochondrial ribosomes, subunit 6 of the ATPase (Atp6p) can be cross-linked to Atp10p. This interaction is required for the integration of Atp6p into a partially assembled subcomplex of the ATPase. Pulse labeling and chase of mitochondrial translation products in vivo indicate that Atp6p is less stable and more rapidly degraded in an atp10 null mutant than in wild type. Based on these observations, we propose Atp10p to be an Atp6p-specific chaperone that facilitates the incorporation of Atp6p into an intermediate subcomplex of ATPase subunits.
| Original language | English |
|---|---|
| Pages (from-to) | 19775-19780 |
| Number of pages | 6 |
| Journal | Journal of Biological Chemistry |
| Volume | 279 |
| Issue number | 19 |
| DOIs | |
| State | Published - May 7 2004 |
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ASJC Scopus subject areas
- Biochemistry
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Atp10p Assists Assembly of Atp6p into the F0 Unit of the Yeast Mitochondrial ATPase. / Tzagoloff, Alexander; Barrientos, Antonio; Neupert, Walter; Herrmann, Johannes M.
In: Journal of Biological Chemistry, Vol. 279, No. 19, 07.05.2004, p. 19775-19780.Research output: Contribution to journal › Article
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TY - JOUR
T1 - Atp10p Assists Assembly of Atp6p into the F0 Unit of the Yeast Mitochondrial ATPase
AU - Tzagoloff, Alexander
AU - Barrientos, Antonio
AU - Neupert, Walter
AU - Herrmann, Johannes M.
PY - 2004/5/7
Y1 - 2004/5/7
N2 - The F0F1-ATPase complex of yeast mitochondria contains three mitochondrial and at least 17 nuclear gene products. The coordinate assembly of mitochondrial and cytosolic translation products relies on chaperones and specific factors that stabilize the pools of some unassembled subunits. Atp10p was identified as a mitochondrial inner membrane component necessary for the biogenesis of the hydrophobic F0 sector of the ATPase. Here we show that, following its synthesis on mitochondrial ribosomes, subunit 6 of the ATPase (Atp6p) can be cross-linked to Atp10p. This interaction is required for the integration of Atp6p into a partially assembled subcomplex of the ATPase. Pulse labeling and chase of mitochondrial translation products in vivo indicate that Atp6p is less stable and more rapidly degraded in an atp10 null mutant than in wild type. Based on these observations, we propose Atp10p to be an Atp6p-specific chaperone that facilitates the incorporation of Atp6p into an intermediate subcomplex of ATPase subunits.
AB - The F0F1-ATPase complex of yeast mitochondria contains three mitochondrial and at least 17 nuclear gene products. The coordinate assembly of mitochondrial and cytosolic translation products relies on chaperones and specific factors that stabilize the pools of some unassembled subunits. Atp10p was identified as a mitochondrial inner membrane component necessary for the biogenesis of the hydrophobic F0 sector of the ATPase. Here we show that, following its synthesis on mitochondrial ribosomes, subunit 6 of the ATPase (Atp6p) can be cross-linked to Atp10p. This interaction is required for the integration of Atp6p into a partially assembled subcomplex of the ATPase. Pulse labeling and chase of mitochondrial translation products in vivo indicate that Atp6p is less stable and more rapidly degraded in an atp10 null mutant than in wild type. Based on these observations, we propose Atp10p to be an Atp6p-specific chaperone that facilitates the incorporation of Atp6p into an intermediate subcomplex of ATPase subunits.
UR - http://www.scopus.com/inward/record.url?scp=2442489927&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=2442489927&partnerID=8YFLogxK
U2 - 10.1074/jbc.M401506200
DO - 10.1074/jbc.M401506200
M3 - Article
C2 - 14998992
AN - SCOPUS:2442489927
VL - 279
SP - 19775
EP - 19780
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 19
ER -