Protein Domain : Photosystem I Ycf4, assembly IPR003359

Type  Family
Description  Photosystem I (PSI) is a large protein complex embedded within the photosynthetic thylakoid membrane formed by a core complex, peripheral light-harvesting complexes (LHCIs) and cofactors. It consists of 15 core and 4 LHCI subunits, ~150 chlorophylls (a and b) molecules, 2 phylloquinones, and 3 Fe4S4-clusters [ ]. The three dimensional structure of the PSI complex has been resolved at 2.5 A [], which allows the precise localisation of each cofactor. PSI together with photosystem II (PSII) catalyses the light-induced steps in oxygenic photosynthesis - a process found in cyanobacteria, eukaryotic algae (e.g. red algae, green algae) and higher plants.To date, three thylakoid proteins involved in the stable accumulation of PSI have been identified: BtpA ( ) [ ], Ycf3 [, ], and Ycf4 []. Because translation of the psaA and psaB mRNAs encoding the two reaction centre polypeptides, of PSI and PSII respectively, is not affected in mutant strains lacking functional ycf3 and ycf4, the products of these two genes appear to act at a post-translational step of PSI biosynthesis. The BtpA protein appears to act at the level of PSI stabilisation []. It is an extrinsic membrane protein located on the cytoplasmic side of the thylakoid membrane [, ]. Homologs of BtpA are found in the crenarchaeota and euryarchaeota, where their function remains unknown. The Ycf4 protein is firmly associated with the thylakoid membrane, presumably through a transmembrane N-terminal domain [, ]. Together with Ycf3, it forms a core PSI assembly apparatus as an auxiliary factor. The Ycf3 is a TPR-containing protein loosely associated with the thylakoid membrane and, with its interacting partner Y3IP1, facilitates the assembly of reaction centre subunits. Ycf4 facilitates the integration of peripheral PSI subunits and LHCIs into the PSI reaction centre subcomplex [ ].
Short Name  PSI_Ycf4_assembly

0 Child Features

1 Gene Families

9 Genes

4 Ontology Annotations

0 Parent Features

2 Publications

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