The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I.

J Knoetzel, D J Simpson

Department of Physiology, Carlsberg Laboratory, Copenhagen Valby, Denmark.

Plant molecular biology 1993 May

filter terms:

A cDNA clone encoding a 15,501 Da photosystem I (PSI) subunit of barley was isolated using an oligonucleotide based on the NH2-terminal amino acid sequence of the isolated protein. The polypeptide, which migrates with an apparent molecular mass of 9.5 kDa on denaturing SDS-PAGE, has been designated PSI-N, and the corresponding gene is PsaN. Analysis of the deduced protein sequence indicates a mature protein of 85 amino acid residues and a molecular mass of 9818 Da. PSI-N is a hydrophilic, extrinsic protein with no predicted membrane-spanning regions. The transit peptide of 60 residues (5683 Da) contains a predicted hydrophobic alpha-helix, suggesting that the protein is routed into the thylakoid lumen. Thus, PSI-N is the second known lumenal protein component associated with PSI, together with PSI-F.

Citation

J Knoetzel, D J Simpson. The primary structure of a cDNA for PsaN, encoding an extrinsic lumenal polypeptide of barley photosystem I. Plant molecular biology. 1993 May;22(2):337-45