» Articles » PMID: 11274447

VIPP1, a Nuclear Gene of Arabidopsis Thaliana Essential for Thylakoid Membrane Formation

Overview
Specialty Science
Date 2001 Mar 29
PMID 11274447
Citations 123
Authors
Affiliations
Soon will be listed here.
Abstract

The conversion of light to chemical energy by the process of photosynthesis is localized to the thylakoid membrane network in plant chloroplasts. Although several pathways have been described that target proteins into and across the thylakoids, little is known about the origin of this membrane system or how the lipid backbone of the thylakoids is transported and fused with the target membrane. Thylakoid biogenesis and maintenance seem to involve the flow of membrane elements via vesicular transport. Here we show by mutational analysis that deletion of a single gene called VIPP1 (vesicle-inducing protein in plastids 1) is deleterious to thylakoid membrane formation. Although VIPP1 is a hydrophilic protein it is found in both the inner envelope and the thylakoid membranes. In VIPP1 deletion mutants vesicle formation is abolished. We propose that VIPP1 is essential for the maintenance of thylakoids by a transport pathway not previously recognized.

Citing Articles

Chloroplast Vesiculation and Induced and Expression During Tomato Flower Pedicel Abscission.

Znidaric M, Zagorscak M, Ramsak Z, Stare K, Chersicola M, Novak M Plant Direct. 2025; 9(1):e70035.

PMID: 39790709 PMC: 11710935. DOI: 10.1002/pld3.70035.


Mechanism for Vipp1 spiral formation, ring biogenesis, and membrane repair.

Naskar S, Merino A, Espadas J, Singh J, Roux A, Colom A Nat Struct Mol Biol. 2024; .

PMID: 39528797 DOI: 10.1038/s41594-024-01401-8.


Monomer unfolding of a bacterial ESCRT-III superfamily member is coupled to oligomer disassembly.

Quarta N, Bhandari T, Girard M, Hellmann N, Schneider D Protein Sci. 2024; 33(11):e5187.

PMID: 39470325 PMC: 11520248. DOI: 10.1002/pro.5187.


Structural basis for Vipp1 membrane binding: from loose coats and carpets to ring and rod assemblies.

Junglas B, Kartte D, Kutzner M, Hellmann N, Ritter I, Schneider D Nat Struct Mol Biol. 2024; .

PMID: 39379528 DOI: 10.1038/s41594-024-01399-z.


The cyanobacterial protein VIPP1 forms ESCRT-III-like structures on lipid bilayers.

Pan S, Gries K, Engel B, Schroda M, Haselwandter C, Scheuring S Nat Struct Mol Biol. 2024; .

PMID: 39060677 PMC: 11762370. DOI: 10.1038/s41594-024-01367-7.


References
1.
Li H, Kaneko Y, Keegstra K . Molecular cloning of a chloroplastic protein associated with both the envelope and thylakoid membranes. Plant Mol Biol. 1994; 25(4):619-32. DOI: 10.1007/BF00029601. View

2.
Hay J, Scheller R . SNAREs and NSF in targeted membrane fusion. Curr Opin Cell Biol. 1997; 9(4):505-12. DOI: 10.1016/s0955-0674(97)80026-9. View

3.
Westphal S, Heins L, Soll J, Vothknecht U . Vipp1 deletion mutant of Synechocystis: a connection between bacterial phage shock and thylakoid biogenesis?. Proc Natl Acad Sci U S A. 2001; 98(7):4243-8. PMC: 31210. DOI: 10.1073/pnas.061501198. View

4.
Meurer J, Meierhoff K, Westhoff P . Isolation of high-chlorophyll-fluorescence mutants of Arabidopsis thaliana and their characterisation by spectroscopy, immunoblotting and northern hybridisation. Planta. 1996; 198(3):385-96. DOI: 10.1007/BF00620055. View

5.
Wollman , Minai , Nechushtai . The biogenesis and assembly of photosynthetic proteins in thylakoid membranes1 . Biochim Biophys Acta. 1999; 1411(1):21-85. DOI: 10.1016/s0005-2728(99)00043-2. View