C1ORF123 is a human hypothetical protein found in open reading frame 123 of chromosome 1. The protein belongs to the DUF866 protein family comprising eukaryote-conserved proteins with unknown function. Recent proteomic and bioinformatic analyses identified the presence of C1ORF123 in brain, frontal cortex and synapses, as well as its involvement in endocrine function and polycystic ovary syndrome (PCOS), indicating the importance of its biological role. In order to provide a better understanding of the biological function of the human C1ORF123 protein, the characterization and analysis of recombinant C1ORF123 (rC1ORF123), including overexpression and purification, verification by mass spectrometry and a Western blot using anti-C1ORF123 antibodies, crystallization and X-ray diffraction analysis of the protein crystals, are reported here. The rC1ORF123 protein was crystallized by the hanging-drop vapor-diffusion method with a reservoir solution comprised of 20% PEG 3350, 0.2 M magnesium chloride hexahydrate, 0.1 M sodium citrate pH 6.5. The crystals diffracted to 1.9 Å resolution and belonged to an orthorhombic space group with unit-cell parameters a = 59.32, b = 65.35, c = 95.05 Å. The calculated Matthews coefficient (VM) value of 2.27 Å(3) Da(-1) suggests that there are two molecules per asymmetric unit, with an estimated solvent content of 45.7%.
Climate change and rapid urbanization are dramatically altering coastal ecosystems worldwide, with significant implications for land surface temperatures (LST) and carbon stock concentration (CSC). This study investigates the impacts of day and night time LST dynamics on CSC in Cox's Bazar, Bangladesh, from 1996 to 2021, with future projections to 2041. Using Landsat and MODIS imagery, we found that mean daytime LST increased by 3.57 °C over the 25-year period, while nighttime LST showed a slight decrease of 0.05 °C. Concurrently, areas with no carbon storage increased by 355.78%, while high and very high CSC zones declined by 14.15% and 47.78%, respectively. The Integrated Valuation of Ecosystem Services and Tradeoffs (InVEST) model estimated a 28.64 km2 reduction in high CSC areas from 1996 to 2021. Statistical analysis revealed strong negative correlations between LST and vegetation indices (R2 = -0.795 to -0.842, p 32 °C, while areas with LST <24 °C may decrease to 1.68%. These observations underscore the pressing necessity for sustainable strategies in urban planning and conservation in swiftly evolving coastal areas, especially considering the challenges posed by climate change and population growth.
Proteins of the DUF866 superfamily are exclusively found in eukaryotic cells. A member of the DUF866 superfamily, C1ORF123, is a human protein found in the open reading frame 123 of chromosome 1. The physiological role of C1ORF123 is yet to be determined. The only available protein structure of the DUF866 family shares just 26% sequence similarity and does not contain a zinc binding motif. Here, we present the crystal structure of the recombinant human C1ORF123 protein (rC1ORF123). The structure has a 2-fold internal symmetry dividing the monomeric protein into two mirrored halves that comprise of distinct electrostatic potential. The N-terminal half of rC1ORF123 includes a zinc-binding domain interacting with a zinc ion near to a potential ligand binding cavity. Functional studies of human C1ORF123 and its homologue in the fission yeast Schizosaccharomyces pombe (SpEss1) point to a role of DUF866 protein in mitochondrial oxidative phosphorylation.