Calculations of liquid helium and neon VUV emission spectra, self-absorption and scattering for a neutrino detector

To evaluate the feasibility of the recently proposed detection scheme of low energy neutrinos released from the Sun and supernovae called CLEAN, Cryogenic Low Energy Astrophysics with Noble Gases, which relies on the transparency of noble-gas cryogenic liquids to VUV radiation produced by neutrinos, we analyze theoretically VUV emission, self-absorption, and scattering of liquid helium and neon, primary candidates for CLEAN. Owing to strong repulsion of noble-gas atoms in the ground states at the equilibrium distance of the relevant excited state, the emission spectrum is substantially shifted from the absorption spectrum, and in principle the absorption is expected very small, allowing building large detectors. Our analysis, however, shows that the self-absorption and Rayleigh scattering are comparable to the size of the proposed detector. Our theoretical emission spectra are found in agreement with experimental observations although some deviation exists due to binary-interaction approximation, and our ab initio Rayleigh scattering lengths are found in agreement with other calculations based on the extrapolation of experimental refraction indices. The absorption process can result in either re-emission, which conserves the number of photons but delays their escape from the liquid, or in non-radiative quenching

Peripherin-2 and Rom-1 have opposing effects on rod outer segment targeting of retinitis pigmentosa-linked peripherin-2 mutants

Mutations in the photoreceptor outer segment (OS) specific peripherin-2 lead to autosomal dominant retinitis pigmentosa (adRP). By contrast, mutations in the peripherin-2 homolog Rom-1 cause digenic RP in combination with certain heterozygous mutations in peripherin-2. The mechanisms underlying the differential role of peripherin-2 and Rom-1 in RP pathophysiology remained elusive so far. Here, focusing on two adRP-linked peripherin-2 mutants, P210L and C214S, we analyzed the binding characteristics, protein assembly, and rod OS targeting of wild type (per(WT)), mutant peripherin-2 (per(MT)), or Rom-1 complexes, which can be formed in patients heterozygous for peripherin-2 mutations. Both mutants are misfolded and lead to decreased binding to per(WT) and Rom-1. Furthermore, both mutants are preferentially forming non-covalent per(MT)-per(MT), per(WT)-per(MT), and Rom-1-per(MT) dimers. However, only per(WT)-per(MT), but not per(MT)-per(MT) or Rom-1-per(MT) complexes could be targeted to murine rod OS. Our study provides first evidence that non-covalent per(WT)-per(MT) dimers can be targeted to rod OS. Finally, our study unravels unexpected opposing roles of per(WT) and Rom-1 in rod OS targeting of adRP-linked peripherin-2 mutants and suggests a new treatment strategy for the affected individuals

RPGR ORF15 isoform co-localizes with RPGRIP1 at centrioles and basal bodies and interacts with nucleophosmin.

The ORF15 isoform of RPGR (RPGR ORF15 ) and RPGR interacting protein 1 (RPGRIP1) are mutated in a variety of retinal dystrophies but their functions are poorly understood. Here, we show that in cultured mammalian cells both RPGR ORF15 and RPGRIP1 localize to centrioles. These localizations are resistant to the microtubule destabilizing drug nocodazole and persist throughout the cell cycle. RPGR and RPGRIP1 also co-localize at basal bodies in cells with primary cilia. The C-terminal (C2) domain of RPGR ORF15 (ORF15 C2 ) is highly conserved across 13 mammalian species, suggesting that it is a functionally important domain. Using matrix-assisted laser desorption ionization time-of-flight mass spectrometry, we show that this domain interacts with a 40 kDa shuttling protein nucleophosmin (NPM). The RPGR ORF15 -NPM interaction was confirmed by (i) yeast two-hybrid analyses; (ii) binding of both recombinant and native HeLa cell NPM to RPGR ORF15 fusion proteins in vitro; (iii) co-immunoprecipitation of native NPM, RPGR ORF15 and RPGRIP1 from bovine retinal extracts and of native HeLa cell NPM and transfected RPGR ORF15 from cultured cells and (iv) co-localization of NPM and RPGR ORF15 at metaphase centrosomes in cultured cells. NPM is a multifunctional protein chaperone that shuttles between the nucleoli and the cytoplasm and has been associated with licensing of centrosomal division. RPGR and RPGRIP1 join a growing number of centrosomal proteins involved in human disease