The 15kDa forms of the apo-peridinin-chlorophyll a protein (PCP) show high 
identity with the apo-32kDa PCP forms, and have similar N-terminal leaders and 
gene arrangements

Hiller, R. G.; Crossley, L. G.; Wrench, P. M.; Santucci, N.; Hofmann, Eckhard

doi:10.1007/s004380100551

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The 15kDa forms of the apo-peridinin-chlorophyll a protein (PCP) show high identity with the apo-32kDa PCP forms, and have similar N-terminal leaders and gene arrangements

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Hofmann, Eckhard
Max Planck Research Group Ion Channel Structure (Dean R. Madden), Max Planck Institute for Medical Research, Max Planck Society;

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Citation

Hiller, R. G., Crossley, L. G., Wrench, P. M., Santucci, N., & Hofmann, E. (2001). The 15kDa forms of the apo-peridinin-chlorophyll a protein (PCP) show high identity with the apo-32kDa PCP forms, and have similar N-terminal leaders and gene arrangements. Molecular Genetics and Genomics, 266, 254-259. doi:10.1007/s004380100551.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-EC33-0

Abstract

Full-length genomic sequences encoding apo-peridinin-chlorophyll a proteins (PCPs) from Heterocapsa pygmaea have been obtained by PCR. Two of the derived mature proteins of 150 residues have molecular masses of 15,795 and 15,780, respectively. Contrary to an earlier report, these show a high degree of identity (~70%) over the whole of both domains to the mature 32-kDa PCP forms. The two genes lack introns, are arranged in tandem and separated by 526 bp. A putative N-terminal extension with three domains characteristic of a signal sequence, a chloroplast-targeting sequence and a thylakoid lumen-directing sequence, is present. Modelling of the Heterocapsa PCP amino acid sequence on to the high-resolution structure available for Amphidinium PCP shows that the main differences between two forms are in trimer contact regions.