Abstract
Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore. The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain and is stably associated with the channel protein Tom40 (refs 11-13). Here we report the unexpected observation that a yeast strain can survive without Tom22, although it is strongly reduced in growth and the import of mitochondrial proteins. Tom22 is a multifunctional protein that is required for the higher-level organization of the TOM machinery. In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating. The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70. Thus a preprotein translocase can combine receptor functions with distinct organizing roles in a multidomain protein.
| Original language | English |
|---|---|
| Pages (from-to) | 485-489 |
| Number of pages | 5 |
| Journal | Nature |
| Volume | 401 |
| Issue number | 6752 |
| DOIs | |
| Publication status | Published - 30 Sep 1999 |
| Externally published | Yes |
Cite this
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Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase. / Van Wilpe, Sandra; Ryan, Michael T.; Hill, Kerstin; Maarse, Ammy C.; Meisinger, Chris; Brix, Jan; Dekker, Peter J.T.; Moczko, Martin; Wagner, Richard; Meijer, Michiel; Gulard, Bernard; Hönlinger, Angelika; Pfanner, Nikolaus.
In: Nature, Vol. 401, No. 6752, 30.09.1999, p. 485-489.Research output: Contribution to journal › Article › Research › peer-review
TY - JOUR
T1 - Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase
AU - Van Wilpe, Sandra
AU - Ryan, Michael T.
AU - Hill, Kerstin
AU - Maarse, Ammy C.
AU - Meisinger, Chris
AU - Brix, Jan
AU - Dekker, Peter J.T.
AU - Moczko, Martin
AU - Wagner, Richard
AU - Meijer, Michiel
AU - Gulard, Bernard
AU - Hönlinger, Angelika
AU - Pfanner, Nikolaus
PY - 1999/9/30
Y1 - 1999/9/30
N2 - Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore. The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain and is stably associated with the channel protein Tom40 (refs 11-13). Here we report the unexpected observation that a yeast strain can survive without Tom22, although it is strongly reduced in growth and the import of mitochondrial proteins. Tom22 is a multifunctional protein that is required for the higher-level organization of the TOM machinery. In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating. The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70. Thus a preprotein translocase can combine receptor functions with distinct organizing roles in a multidomain protein.
AB - Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore. The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain and is stably associated with the channel protein Tom40 (refs 11-13). Here we report the unexpected observation that a yeast strain can survive without Tom22, although it is strongly reduced in growth and the import of mitochondrial proteins. Tom22 is a multifunctional protein that is required for the higher-level organization of the TOM machinery. In the absence of Tom22, the translocase dissociates into core complexes, representing the basic import units, but lacks a tight control of channel gating. The single membrane anchor of Tom22 is required for a stable interaction between the core complexes, whereas its cytosolic domain serves as docking point for the peripheral receptors Tom20 and Tom70. Thus a preprotein translocase can combine receptor functions with distinct organizing roles in a multidomain protein.
UR - http://www.scopus.com/inward/record.url?scp=0033619269&partnerID=8YFLogxK
U2 - 10.1038/46802
DO - 10.1038/46802
M3 - Article
VL - 401
SP - 485
EP - 489
JO - Nature
JF - Nature
SN - 0028-0836
IS - 6752
ER -