Buchumschlag

Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction

Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding prote...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Horn, Annemarie (VerfasserIn) , Hennig, Janosch (VerfasserIn) , Ahmed, Yasar Luqman (VerfasserIn) , Stier, Gunter (VerfasserIn) , Wild, Klemens (VerfasserIn) , Sattler, Michael (VerfasserIn) , Sinning, Irmgard (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 16 Nov 2015
In: Nature Communications
Year: 2015, Jahrgang: 6
ISSN:2041-1723
DOI:10.1038/ncomms9875
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1038/ncomms9875
Verlag, lizenzpflichtig, Volltext: https://www.nature.com/articles/ncomms9875
Volltext
Verfasserangaben:Annemarie Horn, Janosch Hennig, Yasar L. Ahmed, Gunter Stier, Klemens Wild, Michael Sattler, Irmgard Sinning
Beschreibung
Zusammenfassung:Canonical membrane protein biogenesis requires co-translational delivery of ribosome-associated proteins to the Sec translocase and depends on the signal recognition particle (SRP) and its receptor (SR). In contrast, high-throughput delivery of abundant light-harvesting chlorophyll a,b-binding proteins (LHCPs) in chloroplasts to the Alb3 insertase occurs post-translationally via a soluble transit complex including the cpSRP43/cpSRP54 heterodimer (cpSRP). Here we describe the molecular mechanisms of tethering cpSRP to the Alb3 insertase by specific interaction of cpSRP43 chromodomain 3 with a linear motif in the Alb3 C-terminal tail. Combining NMR spectroscopy, X-ray crystallography and biochemical analyses, we dissect the structural basis for selectivity of chromodomains 2 and 3 for their respective ligands cpSRP54 and Alb3, respectively. Negative cooperativity in ligand binding can be explained by dynamics in the chromodomain interface. Our study provides a model for membrane recruitment of the transit complex and may serve as a prototype for a functional gain by the tandem arrangement of chromodomains.
Beschreibung:Gesehen am 14.09.2020
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/ncomms9875

Ähnliche Einträge