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Gene Review

cpcE  -  phycobilisome maturation protein CpcE

Synechococcus elongatus PCC 6301

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Disease relevance of cpcE


High impact information on cpcE

  • When two genes in the phycocyanin operon of this organism, cpcE and cpcF, are inactivated by insertion, together or separately, the surprising result is elimination of correct bilin attachment at only one site, that on the alpha subunit of phycocyanin [2].
  • A mutated cpcA gene containing this substitution was constructed by site-directed mutagenesis and transformed, along with cpcB, into a cpcBAC deletion strain containing an insertionally inactivated cpcE [3].
  • Analysis of the phycocyanin from a cpcE pseudo-revertant, which produced a near wild-type level of phycocyanin with alpha subunit carrying PCB, revealed a single amino acid substitution, alpha-Tyr129----Cys [3].

Chemical compound and disease context of cpcE

  • The cpcE and cpcF genes were separately inactivated by insertion of a kanamycin resistance cassette in Synechococcus sp. PCC 7942 to generate mutants R2EKM and R2FKM, respectively, both of which display a substantial reduction in spectroscopically detectable phycocyanin [1].
  • In the cyanobacterium Synechococcus sp. PCC 7002, the addition of phycocyanobilin to apo-alpha PC is catalyzed by the protein products of the cpcE and cpcF genes [4].

Biological context of cpcE


Other interactions of cpcE

  • The levels of beta- and alpha-phycocyanin polypeptides were reduced in the R2EKM and R2FKM mutants although the phycocyanin and linker genes are transcribed at normal levels in the mutants as in the wild type indicating the requirement of the functional cpcE and cpcF genes for normal accumulation of phycocyanin [1].


  1. Cloning of the cpcE and cpcF genes from Synechococcus sp. PCC 6301 and their inactivation in Synechococcus sp. PCC 7942. Bhalerao, R.P., Lind, L.K., Gustafsson, P. Plant Mol. Biol. (1994) [Pubmed]
  2. Phycocyanin alpha-subunit phycocyanobilin lyase. Fairchild, C.D., Zhao, J., Zhou, J., Colson, S.E., Bryant, D.A., Glazer, A.N. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  3. Characterization of phycocyanin produced by cpcE and cpcF mutants and identification of an intergenic suppressor of the defect in bilin attachment. Swanson, R.V., Zhou, J., Leary, J.A., Williams, T., de Lorimier, R., Bryant, D.A., Glazer, A.N. J. Biol. Chem. (1992) [Pubmed]
  4. Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase. Fairchild, C.D., Glazer, A.N. J. Biol. Chem. (1994) [Pubmed]
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