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Vol. 20, Issue 21, 4620-4628, November 1, 2009

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The Vesicle-inducing Protein 1 from Synechocystis sp. PCC 6803 Organizes into Diverse Higher-Ordered Ring Structures

Eva Fuhrmann^*,, Jelle B. Bultema, Uwe Kahmann, Eva Rupprecht^*, Egbert J. Boekema, and Dirk Schneider^*

*Institut für Biochemie und Molekularbiologie, ZBMZ, Fakultät für Biologie, Albert-Ludwigs-Universität, 79104 Freiburg, Germany; Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, 9747 AG Groningen, The Netherlands; and Fakultät für Biologie, Universität Bielefeld, D-33501 Bielefeld, Germany

Submitted April 20, 2009; Revised September 10, 2009; Accepted September 15, 2009
Monitoring Editor: Reid Gilmore

The vesicle-inducing protein in plastids 1 (Vipp1) was found to be involved in thylakoid membrane formation in chloroplasts and cyanobacteria. In contrast to chloroplasts, it has been suggested that in cyanobacteria the protein is only tightly associated with the cytoplasmic membrane. In the present study we analyze and describe the subcellular localization and the oligomeric organization of Vipp1 from the cyanobacterium Synechocystis PCC 6803. Vipp1 forms stable dimers and higher-ordered oligomers in the cytoplasm as well as at both the cytoplasmic and thylakoid membrane. Vipp1 oligomers are organized in ring structures with a variable diameter of 25–33 nm and corresponding calculated molecular masses of 1.6–2.2 MDa. Six different types of rings were found with an unusual 12–17-fold symmetrical conformation. The simultaneous existence of multiple types of rings is very unusual and suggests a special function of Vipp1. Involvement of diverse ring structures in vesicle formation is suggested.

Address correspondence to: Dirk Schneider (Dirk.Schneider{at}biochemie.uni-freiburg.de).

Abbreviations used: BN, blue-native; DDM, n-dodecyl-β-D-maltoside; EM, electron microscopy; SEC, size exclusion chromatography; Vipp1, vesicle-inducing protein in plastids 1.