» Articles » PMID: 16679460

One of Two Alb3 Proteins is Essential for the Assembly of the Photosystems and for Cell Survival in Chlamydomonas

Overview
Journal Plant Cell
Specialties Biology
Cell Biology
Date 2006 May 9
PMID 16679460
Citations 60
Authors
Affiliations
Soon will be listed here.
Abstract

Proteins of the YidC/Oxa1p/ALB3 family play an important role in inserting proteins into membranes of mitochondria, bacteria, and chloroplasts. In Chlamydomonas reinhardtii, one member of this family, Albino3.1 (Alb3.1), was previously shown to be mainly involved in the assembly of the light-harvesting complex. Here, we show that a second member, Alb3.2, is located in the thylakoid membrane, where it is associated with large molecular weight complexes. Coimmunoprecipitation experiments indicate that Alb3.2 interacts with Alb3.1 and the reaction center polypeptides of photosystem I and II as well as with VIPP1, which is involved in thylakoid formation. Moreover, depletion of Alb3.2 by RNA interference to 25 to 40% of wild-type levels leads to a reduction in photosystems I and II, indicating that the level of Alb3.2 is limiting for the assembly and/or maintenance of these complexes in the thylakoid membrane. Although the levels of several photosynthetic proteins are reduced under these conditions, other proteins are overproduced, such as VIPP1 and the chloroplast chaperone pair Hsp70/Cdj2. These changes are accompanied by a large increase in vacuolar size and, after a prolonged period, by cell death. We conclude that Alb3.2 is required directly or indirectly, through its impact on thylakoid protein biogenesis, for cell survival.

Citing Articles

The role of chloroplast SRP54 domains and its C-terminal tail region in post- and co-translational protein transport in vivo.

Bischoff A, Ortelt J, Dunschede B, Zegarra V, Bedrunka P, Bange G J Exp Bot. 2024; 75(18):5734-5749.

PMID: 38989593 PMC: 11427828. DOI: 10.1093/jxb/erae293.


Structure, function, and assembly of PSI in thylakoid membranes of vascular plants.

Rolo D, Schottler M, Sandoval-Ibanez O, Bock R Plant Cell. 2024; 36(10):4080-4108.

PMID: 38848316 PMC: 11449065. DOI: 10.1093/plcell/koae169.


A unifying model for membrane protein biogenesis.

Hegde R, Keenan R Nat Struct Mol Biol. 2024; 31(7):1009-1017.

PMID: 38811793 PMC: 7616256. DOI: 10.1038/s41594-024-01296-5.


Assembly and Repair of Photosystem II in .

Mehra H, Wang X, Russell B, Kulkarni N, Ferrari N, Larson B Plants (Basel). 2024; 13(6).

PMID: 38592843 PMC: 10975043. DOI: 10.3390/plants13060811.


Uncovering the photosystem I assembly pathway in land plants.

Zhang A, Tian L, Zhu T, Li M, Sun M, Fang Y Nat Plants. 2024; 10(4):645-660.

PMID: 38503963 DOI: 10.1038/s41477-024-01658-3.


References
1.
Barkan A, Goldschmidt-Clermont M . Participation of nuclear genes in chloroplast gene expression. Biochimie. 2000; 82(6-7):559-72. DOI: 10.1016/s0300-9084(00)00602-7. View

2.
Wilde A, Hartel H, Hubschmann T, Hoffmann P, Shestakov S, Borner T . Inactivation of a Synechocystis sp strain PCC 6803 gene with homology to conserved chloroplast open reading frame 184 increases the photosystem II-to-photosystem I ratio. Plant Cell. 1995; 7(5):649-58. PMC: 160811. DOI: 10.1105/tpc.7.5.649. View

3.
Pasch J, Nickelsen J, Schunemann D . The yeast split-ubiquitin system to study chloroplast membrane protein interactions. Appl Microbiol Biotechnol. 2005; 69(4):440-7. DOI: 10.1007/s00253-005-0029-3. View

4.
Keegstra K, Cline K . Protein import and routing systems of chloroplasts. Plant Cell. 1999; 11(4):557-70. PMC: 144212. DOI: 10.1105/tpc.11.4.557. View

5.
Bonnefoy N, Chalvet F, Hamel P, SLONIMSKI P, Dujardin G . OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis. J Mol Biol. 1994; 239(2):201-12. DOI: 10.1006/jmbi.1994.1363. View