Tom22 is a multifunctional organizer of the mitochondrial preprotein translocase
Autor(en): | van Wilpe, S Ryan, MT Hill, K Maarse, AC Meisinger, C Brix, J Dekker, PJT Moczko, M Wagner, R Meijer, M Guiard, B Honlinger, A Pfanner, N |
Stichwörter: | CELL VIABILITY; CHANNEL; COMPONENT; DOMAINS; GENERAL IMPORT PORE; MOM22; Multidisciplinary Sciences; NEUROSPORA-CRASSA; OUTER-MEMBRANE PROTEIN; RECEPTOR COMPLEX; Science & Technology - Other Topics; YEAST MITOCHONDRIA | Erscheinungsdatum: | 1999 | Herausgeber: | MACMILLAN MAGAZINES LTD | Journal: | NATURE | Volumen: | 401 | Ausgabe: | 6752 | Startseite: | 485 | Seitenende: | 489 | Zusammenfassung: | Mitochondrial preproteins are imported by a multisubunit translocase of the outer membrane (TOM), including receptor proteins and a general import pore(1-5). The central receptor Tom22 binds preproteins through both its cytosolic domain and its intermembrane space domain(6-10) 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. |
ISSN: | 00280836 | DOI: | 10.1038/46802 |
Zur Langanzeige
Seitenaufrufe
4
Letzte Woche
0
0
Letzter Monat
0
0
geprüft am 01.06.2024