Eser, Markus; Ehrmann, Michael:
SecA-dependent quality control of intracellular protein localization
2003
In: Proceedings of the National Academy of Sciences of the United States of America : PNAS, Jg. 100 (2003), Heft 23, S. 13231 - 13234
Artikel/Aufsatz in Zeitschrift / Fach: Biologie
Fakultät für Biologie
Titel:
SecA-dependent quality control of intracellular protein localization
Autor(in):
Eser, Markus; Ehrmann, Michael im Online-Personal- und -Vorlesungsverzeichnis LSF anzeigen
Erscheinungsjahr:
2003
Erschienen in:
Proceedings of the National Academy of Sciences of the United States of America : PNAS, Jg. 100 (2003), Heft 23, S. 13231 - 13234
ISSN:
Link URL:

Abstract:

Complex secretion machineries mediate protein translocation across cellular membranes. These machines typically recognize their substrates via signal sequences, which are required for proper targeting to the translocon. We report that during posttranslational secretion the widely conserved targeting factor SecA performs a quality-control function that is based on a general chaperone activity. This quality-control mechanism involves assisted folding of signal sequenceless proteins, thereby excluding them from the secretion process. These results suggest that SecA channels proteins into one of two key pathways, posttranslational secretion or folding in the cytoplasm. Implications of this finding for intracellular protein localization are discussed.