Short C-terminal Musashi-1 proteins regulate pluripotency states in embryonic stem cells.

The RNA-binding protein Musashi-1 (MSI1) regulates the proliferation and differentiation of adult stem cells. However, its role in embryonic stem cells (ESCs) and early embryonic development remains poorly understood. Here, we report the presence of short C-terminal MSI1 (MSI1-C) proteins in early mouse embryos and mouse ESCs, but not in human ESCs, under conventional culture conditions. In mouse embryos and mESCs, deletion of MSI1-C together with full-length MSI1 causes early embryonic developmental arrest and pluripotency dissolution. MSI1-C is induced upon naive induction and facilitates hESC naive pluripotency acquisition, elevating the pluripotency of primed hESCs toward a formative-like state. MSI1-C proteins are nuclear localized and bind to RNAs involved in DNA-damage repair (including MLH1, BRCA1, and MSH2), conferring on hESCs better survival in human-mouse interspecies cell competition and prolonged ability to form blastoids. This study identifies MSI1-C as an essential regulator in ESC pluripotency states and early embryonic development.

Preparation of sludge-cyanobacteria composite carbon for synergistically enhanced co-removal of Cu(II) and Cr(VI).

Traditional sludge disposal is currently restricted by the risk of secondary pollution. Sludge carbon material has gained widespread attention because of its low cost and environmentally sustainable properties. However, owing to the high ash content and low-energy density of sludge, sludge pyrolysis alone has certain limitations, and the performance of carbon materials needs to be improved. Herein, a sludge-cyanobacteria composite carbon (SCC) was easily synthesized, and the adsorption process of Cu(II) and Cr(VI) by SCC was examined. SCC-700-2-50% exhibited a high SBET (1047.54 m2/g) and developed pore structure rich in functional groups (such as -NH, -OH, and C-O). The combination of pore structure and functional groups improved the adsorption performance of SCC. The adsorption processes exhibited a synergistic effect in a binary system: the qm of Cu(II) and Cr(VI) were 386 mg/g and 341 mg/g, respectively, and the selectivity of Cu(II) adsorption by SCC was greater than Cr(VI). The adsorption process, examined by SEM-EDS, FTIR, and XPS analysis, indicated that Cu(II) as a cationic interface strengthens Cr(VI) adsorption through electrostatic interaction, and the anion Cr(VI) created a valid electrostatic shield against the electrostatic repulsion between H+ and Cu(II), facilitating Cu(II) adsorption. SCC had great reusability: Cu(II) and Cr(VI) adsorption capacity were 90% and 84%, of the initial adsorption capacity, respectively, after six cycles. This study demonstrates the prospect of SCC as a valid adsorbent for multiple heavy metal contaminations removal.

Pharmacological Modulation of Melanocortin 1 Receptor Signaling by Mrap Proteins in Xenopus tropicalis.

The melanocortin system consists of five G protein-coupled receptors (MC1R-MC5R), the bidirectional endogenous ligands (MSH and Agouti families), and accessory proteins (MRAP1 and MRAP2). Accumulative studies of vertebrate species find high expression level of melanocortin 1 receptor (MC1R) in the dermal melanocyte and elucidate the essential roles in the skin and fur pigmentation, morphological background adaptation, and stress response. The diploid amphibian Xenopus tropicalis (xt) has been utilized as a fantastic animal model for embryonic development and studies of physiological cryptic colouring and environmental adaptiveness. However, the interaction of xtMc1r signaling with xtMrap proteins has not been assessed yet. In this study, we carried out in silico evolutionary analysis of protein alignment and genetic phylogenetic and genomic synteny of mc1r among various vertebrates. Ubiquitous expression of mrap1 and mrap2 and the co-expression with mc1r transcripts in the skin were clearly observed. Co-immunoprecipitation (ip) and fluorescent complementary approach validated the direct functional interaction of xtMc1r with xtMrap1 or xtMrap2 proteins on the plasma membrane. Pharmacological assay showed the improvement of the constitutive activity and alpha melanocyte-stimulating hormone (α-MSH) stimulated plateau without dramatic alteration of the cell surface translocation of xtMc1r in the presence of xtMrap proteins. Overall, the pharmacological modulation of xtMc1r by dual xtMrap2 proteins elucidated the potential role of this protein complex in the regulation of proper dermal function in amphibian species.