Characterization and N-terminal sequence of a 5 kDa polypeptide in the photosystem I core complex from spinach.

Photosystem I core complexes were isolated from spinach photosystem I particles after heat treatment in the presence of 50% (v/v) ethylene glycol (heat/EG treatment). The core complex from 58 degrees C/EG-treated particles was composed of polypeptides with apparent molecular masses of 63, 60 and 5 kDA; this complex contained the iron sulfur center Fx but lacked center FA and FB. The core complex obtained from the 70 degrees C/EG-treated preparation lacked FX and contained a lesser amount of the 5 kDa polypeptide. The N-terminal amino acid sequence of the 5 kDa polypeptide did not correspond to the sequence derived from any possible reading frame in the chloroplast DNA of liverwort or tobacco. Twelve of the first 29 N-terminal amino acids were hydrophobic, suggesting that this protein is intrinsic to the photosystem I reaction center.