AI Article Synopsis
- Hybrid cluster proteins (HCPs) are metalloproteins containing an iron-sulfur-oxygen cluster, found in all life forms but primarily studied in certain anaerobic parasites and photosynthetic microalgae, notably Chlamydomonas reinhardtii, which has four HCP genes.
- Research indicates that HCPs in C. reinhardtii likely originated from a single alpha proteobacterial gene and expanded through duplication, with studies on HCP1 and HCP3 revealing their unique redox properties and structures.
- Experiments show that both nitrate and darkness significantly increase HCP levels in C. reinhardtii under oxygen-rich conditions, suggesting a connection between HCPs and
Article Abstract
Hybrid cluster proteins (HCPs) are metalloproteins characterized by the presence of an iron-sulfur-oxygen cluster. These proteins occur in all three domains of life. In eukaryotes, HCPs have so far been found only in a few anaerobic parasites and photosynthetic microalgae. With respect to all species harboring an HCP, the green microalga Chlamydomonas reinhardtii stands out by the presence of four HCP genes. The study of the gene and protein structures as well as the phylogenetic analyses strongly support a model in which the HCP family in the alga has emerged from a single gene of alpha proteobacterial origin and then expanded by several rounds of duplications. The spectra and redox properties of HCP1 and HCP3, produced heterologously in Escherichia coli, were analyzed by electron paramagnetic resonance spectroscopy on redox-titrated samples. Both proteins contain a [4Fe-4S]-cluster as well as a [4Fe-2O-2S]-hybrid cluster with paramagnetic properties related to those of HCPs from Desulfovibrio species. Immunoblotting experiments combined with mass spectrometry-based proteomics showed that both nitrate and darkness contribute to the strong upregulation of the HCP levels in C. reinhardtii growing under oxic conditions. The link to the nitrate metabolism is discussed in the light of recent data on the potential role of HCP in S-nitrosylation in bacteria.
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| http://dx.doi.org/10.1111/febs.15025 | DOI Listing |
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