High impact information on CYC2

• The gene, Sco6073 (cyc2), codes for a protein with two sesquiterpene synthase domains, only one of which is required for geosmin biosynthesis, probably via a germacra-1 (10) E,5E-dien-11-ol intermediate generated by the sesquiterpene synthase from farnesyl pyrophosphate [1].
• We propose that CYC2 encodes a factor that increases the efficiency of cytochrome c import into mitochondria [2].
• The intensities of these bands vary according to the gene dosage of CYC2 in various isogenic strains [2].
• Immunoblotting of subcellular fractions suggests that the CYC2 gene product is a mitochondrial protein [2].
• CYC2 encodes a 168-amino-acid open reading frame with at least two potential transmembrane segments [2].

Biological context of CYC2

• Both CYC2 and CYC3 are single-copy genes and expressed in all life cycle stages of the parasite [3].
• To determine if CYC2 is found in a complex with previously identified trypanosome cdc2-related kinases (CRKs), the CYC2 gene was fused to the TY epitope tag, integrated into the trypanosome genome, and expressed under inducible control [3].
• Gene knockout experiments provide evidence that CYC2 is an essential gene, and co-immune precipitations together with a two-hybrid interaction assay demonstrated that CYC2 interacts with CRK3 [3].
• We show that Cyc2p is required for the activity of CCHL toward apocytochrome c and c1 and becomes essential for the heme attachment to apocytochrome c1 carrying a CAPCH instead of CAACH heme binding site [4].

Associations of CYC2 with chemical compounds

• Based on the functional interaction of Cyc2p with CCHL and the presence of a putative FAD-binding site in the protein, we hypothesize that Cyc2p controls the redox chemistry of the heme lyase reaction [5].

Physical interactions of CYC2

• We postulate that, in vivo, Cyc2p interacts with CCHL and is involved in the reduction of heme prior to its ligation to apocytochrome c by CCHL [4].

Other interactions of CYC2

• CYC2 encodes a 24-kDa protein that has sequence identity to the Neurospora crassa PREG1 and the S. cerevisiae PHO80 cyclin [3].
• None of the cyc strains surveyed (cyc1, cyc2, cyc3, cyc4, cyc5, and cyc6) had diminished levels of methylase, although some of them were completely or almost completely deficient in cytochrome c [6].
• Requirements of Cyc2p and the porin, Por1p, for ionic stability and mitochondrial integrity in Saccharomyces cerevisiae [7].

References