Herskovits, Anat A.; Seluanov, Andrei; Rajsbaum, Ricardo; ten Hagen-Jongman, Corinne M.; Henrichs, Tanja; Bochkareva, Elena S.; Phillips, Gregory J.; Probst, Francis J.; Nakae, Taiji; Ehrmann, Michael; Luirink, Joen; Bibi, Eitan:
Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor Fts Y
In: EMBO Reports, Jg. 2 (2001), Heft 11, S. 1040 - 1046
2001Artikel/Aufsatz in Zeitschrift
BiologieFakultät für Biologie
Damit verbunden: 1 Publikation(en)
Titel:
Evidence for coupling of membrane targeting and function of the signal recognition particle (SRP) receptor Fts Y
Autor*in:
Herskovits, Anat A.;Seluanov, Andrei;Rajsbaum, Ricardo;ten Hagen-Jongman, Corinne M.;Henrichs, Tanja;Bochkareva, Elena S.;Phillips, Gregory J.;Probst, Francis J.;Nakae, Taiji;Ehrmann, MichaelUDE
LSF ID
13331
ORCID
0000-0002-1927-260XORCID iD
Sonstiges
der Hochschule zugeordnete*r Autor*in
;
Luirink, Joen;Bibi, Eitan
Erscheinungsjahr:
2001

Abstract:

Recent studies have indicated that FtsY, the signal recognition particle receptor of Escherichia coli, plays a central role in membrane protein biogenesis. For proper function, FtsY must be targeted to the membrane, but its membrane-targeting pathway is unknown. We investigated the relationship between targeting and function of FtsY in vivo, by separating its catalytic domain (NG) from its putative targeting domain (A) by three means: expression of split ftsY, insertion of various spacers between A and NG, and separation of A and NG by in vivo proteolysis. Proteolytic separation of A and NG does not abolish function, whereas separation by long linkers or expression of split ftsY is detrimental. We propose that proteolytic cleavage of FtsY occurs after completion of co-translational targeting and assembly of NG. In contrast, separation by other means may interrupt proper synchronization of co-translational targeting and membrane assembly of NG. The co-translational interaction of FtsY with the membrane was confirmed by in vitro experiments.