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The Plant Cell 18:2419

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IN BRIEF

Pushing the Envelope: The Role of Outer Envelope Proteins PVD1 and PVD2 in Plastid Division

Nancy A. Eckardt, News and Reviews Editor

neckardt{at}aspb.org

Molecular genetic studies in Arabidopsis have defined several nuclear-encoded homologs of cyanobacterial cell division proteins that function in plastid division in photosynthetic eukaryotes, suggesting horizontal transfer from the ancestral cyanobacterial endosymbiont genome to the host genome in evolutionary history. These include the tubulin-like protein FtsZ, which forms a ring structure at the division site, and several other proteins that regulate positioning and stabilization of the FtsZ ring. However, recent work suggests that many genes regulating cyanobacterial cell division were lost after endosymbiosis, and other genes of eukaryotic origin have been recruited to function in plastid division. The best-characterized of these is ARC5, which encodes a member of the dynamin superfamily of eukaryotic membrane-remodeling GTPases that is recruited from patches in the cytosol to the plastid outer envelope surface at the division site. Arabidopsis arc5 mutants exhibit arrest of chloroplast division, suggesting that the protein functions in severing the envelope membranes. Miyagishima et al. (pages 2517–2530) identified two new integral outer envelope membrane proteins, PVD1 and PVD2, through analysis of mutants similar to arc5. The authors present detailed topological and mutational analyses of protein function that show that PVD1 and PVD2 together mediate recruitment of ARC5 to the site of constriction at a late stage of division.


Figure 1
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  		Chloroplasts of pvd mutants appear constricted and larger than those in wild-type plants.

 
Footnotes

www.plantcell.org/cgi/doi/10.1105/tpc.106.181011


Related articles in Plant Cell:

PDV1 and PDV2 Mediate Recruitment of the Dynamin-Related Protein ARC5 to the Plastid Division Site
Shin-ya Miyagishima, John E. Froehlich, and Katherine W. Osteryoung
Plant Cell 2006 18: 2517-2530. [Abstract] [Full Text]  




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