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

Annemarie Horn, Janosch Hennig, Yasar L. Ahmed, Gunter Stier, Klemens Wild, Michael Sattler () and Irmgard Sinning ()
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Annemarie Horn: Heidelberg University Biochemistry Center (BZH), INF 328
Janosch Hennig: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Yasar L. Ahmed: Heidelberg University Biochemistry Center (BZH), INF 328
Gunter Stier: Heidelberg University Biochemistry Center (BZH), INF 328
Klemens Wild: Heidelberg University Biochemistry Center (BZH), INF 328
Michael Sattler: Center for Integrated Protein Science Munich at Biomolecular NMR Spectroscopy, Technische Universität München
Irmgard Sinning: Heidelberg University Biochemistry Center (BZH), INF 328

Nature Communications, 2015, vol. 6, issue 1, 1-11

Abstract: Abstract 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.

Date: 2015
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DOI: 10.1038/ncomms9875

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