Unique constitution of photosystem I with a novel subunit in the cyanobacterium Gloeobacter violaceus PCC 7421.
Constitution of the photosystem I complex isolated from the cyanobacterium Gloeobacter violaceus PCC 7421 was investigated by tricine-urea-SDS-PAGE, followed by peptide mass fingerprinting or N-terminal sequencing. Eight subunits (PsaA, PsaB, PsaC, PsaD, PsaE, PsaF, PsaL and PsaM) were identified as predicted from the genome sequence. A novel subunit (PsaZ) was discovered, but PsaI, PsaJ, PsaK and PsaX were absent. PsaB has a C-terminal extension with 155 amino acids in addition to the conserved region and this domain is similar to the peptidoglycan-binding domain. These results suggest that PS I complexes of G. violaceus have unique structural properties.
Inoue
Hidetoshi
H
Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, Japan.
Tsuchiya
Tohru
T
Satoh
Soichirou
S
Miyashita
Hideaki
H
Kaneko
Takakazu
T
Tabata
Satoshi
S
Tanaka
Ayumi
A
Mimuro
Mamoru
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000302:isolation & purification*; D017124:Conserved Sequence; D000458:Cyanobacteria / Q000235:genetics*; D004591:Electrophoresis, Polyacrylamide Gel; D019143:Evolution, Molecular; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D045331:Photosystem I Protein Complex / Q000737:chemistry* / Q000302:isolation & purification; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D021122:Protein Subunits / Q000737:chemistry*; D020539:Sequence Analysis, Protein; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D001426:Bacterial Proteins; D045331:Photosystem I Protein Complex; D021122:Protein Subunits