Navigation überspringen
Universitätsbibliothek Heidelberg
Status: Bibliographieeintrag

Verfügbarkeit
Standort: ---
Exemplare: ---
heiBIB
 Online-Ressource
Verfasst von:Erez, Elinor [VerfasserIn]   i
 Stjepanović, Goran [VerfasserIn]   i
 Zelazny, Adrian M. [VerfasserIn]   i
 Brügger, Britta [VerfasserIn]   i
 Sinning, Irmgard [VerfasserIn]   i
 Bibi, Eitan [VerfasserIn]   i
Titel:Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo
Verf.angabe:Elinor Erez, Goran Stjepanovic, Adrian M. Zelazny, Britta Brugger, Irmgard Sinning, and Eitan Bibi
E-Jahr:2010
Jahr:18 October 2010
Umfang:7 S.
Fussnoten:Available online 18 October 2010, version of record 4 January 2021 ; Gesehen am 20.03.2023
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : ASBMB Publications, 1905
Jahr Quelle:2010
Band/Heft Quelle:285(2010), 52 vom: Dez., Seite 40508-40514
ISSN Quelle:1083-351X
Abstract:The mechanism underlying the interaction of the Escherichia coli signal recognition particle receptor FtsY with the cytoplasmic membrane has been studied in detail. Recently, we proposed that FtsY requires functional interaction with inner membrane lipids at a late stage of the signal recognition particle pathway. In addition, an essential lipid-binding α-helix was identified in FtsY of various origins. Theoretical considerations and in vitro studies have suggested that it interacts with acidic lipids, but this notion is not yet fully supported by in vivo experimental evidence. Here, we present an unbiased genetic clue, obtained by serendipity, supporting the involvement of acidic lipids. Utilizing a dominant negative mutant of FtsY (termed NG), which is defective in its functional interaction with lipids, we screened for E. coli genes that suppress the negative dominant phenotype. In addition to several unrelated phenotype-suppressor genes, we identified pgsA, which encodes the enzyme phosphatidylglycerophosphate synthase (PgsA). PgsA is an integral membrane protein that catalyzes the committed step to acidic phospholipid synthesis, and we show that its overexpression increases the contents of cardiolipin and phosphatidylglycerol. Remarkably, expression of PgsA also stabilizes NG and restores its biological function. Collectively, our results strongly support the notion that FtsY functionally interacts with acidic lipids.
DOI:doi:10.1074/jbc.M110.140921
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1074/jbc.M110.140921
 Volltext: https://www.sciencedirect.com/science/article/pii/S0021925819762176
 DOI: https://doi.org/10.1074/jbc.M110.140921
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Acidic Lipids
 ffh
 ftsy
 Membrane Lipids
 Membrane Proteins
 Phosphatidylglycerol
 Protein Targeting
 Protein Translocation
 Signal Recognition Particle
 SRP
K10plus-PPN:1839572787
Verknüpfungen:→ Zeitschrift

Permanenter Link auf diesen Titel (bookmarkfähig):  https://katalog.ub.uni-heidelberg.de/titel/69053282   QR-Code
zum Seitenanfang