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The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding

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Abstract

The vesicle-inducing protein in plastids 1 (Vipp1) is an essential component for thylakoid biogenesis in cyanobacteria and chloroplasts. Vipp1 proteins share significant structural similarity with their evolutionary ancestor PspA (bacterial phage shock protein A), namely a predominantly α-helical structure, the formation of oligomeric high molecular weight complexes (HMW-Cs) and a tight association with membranes. Here, we elucidated domains of Vipp1 from Arabidopsis thaliana involved in homo-oligomerization as well as association with chloroplast inner envelope membranes. We could show that the 21 N-terminal amino acids of Vipp1, which form the first α-helix of the protein, are essential for assembly of the 2 MDa HMW-C but are not needed for formation of smaller subcomplexes. Interestingly, removal of this domain also interferes with association of the Vipp1 protein to the inner envelope. Fourier transform infrared spectroscopy of recombinant Vipp1 further indicates that Escherichia coli lipids bind tightly enough that they can be co-purified with the protein. This feature also depends on the presence of the first helix, which strongly supports an interaction of lipids with the Vipp1 HMW-C but not with smaller subcomplexes. Therefore, Vipp1 oligomerization appears to be a prerequisite for its membrane association. Our results further highlight structural differences between Vipp1 and PspA, which might be important in regard to their different function in thylakoid biogenesis and bacterial stress response, respectively.

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Abbreviations

ATR-FTIR:

Attenuated total reflectance Fourier transform infrared spectroscopy

EM:

Electron microscopy

HMW-C:

High molecular weight complex

PspA:

Phage shock protein A

SEC:

Size exclusion chromatography

Vipp1:

Vesicle-inducing protein in plastids 1

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Acknowledgments

This work was supported by grants from the Deutsche Forschungsgemeinschaft to UCV (SFB-TR1, project A6) and PB (BR-1991/2-1).

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Authors and Affiliations

  1. Department of Biology I, Botany, LMU Munich, Großhaderner Str. 2-4, Planegg-Martinsried, 82152, Munich, Germany

    Stephanie Otters, Johanna Hubner, Gerhardt Wanner & Ute C. Vothknecht

  2. Center for Integrated Protein Science (Munich) at the Department of Biology, LMU Munich, Planegg-Martinsried, 82152, Munich, Germany

    Ute C. Vothknecht & Fatima Chigri

  3. Munich University of Applied Sciences, Lothstr. 34, 80335, Munich, Germany

    Paula Braun

Authors
  1. Stephanie Otters
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  2. Paula Braun
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  3. Johanna Hubner
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  4. Gerhardt Wanner
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  5. Ute C. Vothknecht
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  6. Fatima Chigri
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Correspondence to Ute C. Vothknecht.

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A contribution to the Special Issue on Evolution and Biogenesis of Chloroplasts and Mitochondria.

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Otters, S., Braun, P., Hubner, J. et al. The first α-helical domain of the vesicle-inducing protein in plastids 1 promotes oligomerization and lipid binding. Planta 237, 529–540 (2013). https://doi.org/10.1007/s00425-012-1772-1

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  • DOI: https://doi.org/10.1007/s00425-012-1772-1

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