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

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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
    Institute of Structural Biology, Helmholtz Center Munich)

  • 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
    Institute of Structural Biology, Helmholtz Center Munich)

  • Irmgard Sinning

    (Heidelberg University Biochemistry Center (BZH), INF 328)

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.

Suggested Citation

  • Annemarie Horn & Janosch Hennig & Yasar L. Ahmed & Gunter Stier & Klemens Wild & Michael Sattler & Irmgard Sinning, 2015. "Structural basis for cpSRP43 chromodomain selectivity and dynamics in Alb3 insertase interaction," Nature Communications, Nature, vol. 6(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9875
    DOI: 10.1038/ncomms9875
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