66,016 research outputs found

    Fluorescent protein tagging confirms the presence of ribosomal proteins atDrosophilapolytene chromosomes

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    \ud \ud Most ribosomal proteins (RPs) are stoichiometrically incorporated into ribosomal subunits and play essential roles in ribosome biogenesis and function. However, a number of RPs appear to have non-ribosomal functions, which involve direct association with pre-mRNA and transcription factors at transcription sites. The consensus is that the RPs found at these sites are off ribosomal subunits, but observation that different RPs are usually found together suggests that ribosomal or ribosomal-like subunits might be present. Notably, it has previously been reported that antibodies against 20 different RPs stain the same Pol II transcription sites in Drosophila polytene chromosomes. Some concerns, however, were raised about the specificity of the antibodies. To investigate further whether RPs are present at transcription sites in Drosophila, we have generated several transgenic flies expressing RPs (RpS2, RpS5a, RpS9, RpS11, RpS13, RpS18, RpL8, RpL11, RpL32, and RpL36) tagged with either green or red fluorescent protein. Imaging of salivary gland cells showed that these proteins are, as expected, abundant in the cytoplasm as well as in the nucleolus. However, these RPs are also apparent in the nucleus in the region occupied by the chromosomes. Indeed, polytene chromosome immunostaining of a representative subset of tagged RPs confirms the association with transcribed loci. Furthermore, characterization of a strain expressing RpL41 functionally tagged at its native genomic locus with YFP, also showed apparent nuclear accumulation and chromosomal association, suggesting that such a nuclear localization pattern might be a shared feature of RPs and is biologically important. We anticipate that the transgenes described here should provide a useful research tool to visualize ribosomal subunits in Drosophila tissues and to study the non-ribosomal functions of RPs.\u

    Survival of Massive Star-forming Galaxies in Cluster Cores Drives Gas-Phase Metallicity Gradients : The Effects of Ram Pressure Stripping

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    Recent observations of galaxies in a cluster at z=0.35 show that their integrated gas-phase metallicities increase with decreasing cluster-centric distance. To test if ram pressure stripping (RPS) is the underlying cause, we use a semi-analytic model to quantify the "observational bias" that RPS introduces into the aperture-based metallicity measurements. We take integral field spectroscopy of local galaxies, remove gas from their outer galactic disks via RPS, and then conduct mock slit observations of cluster galaxies at z=0.35. Our RPS model predicts a typical cluster-scale metallicity gradient of -0.03 dex/Mpc. By removing gas from the outer galactic disks, RPS introduces a mean metallicity enhancement of +0.02 dex at a fixed stellar mass. This gas removal and subsequent quenching of star formation preferentially removes low mass cluster galaxies from the observed star-forming population. As only the more massive star-forming galaxies survive to reach the cluster core, RPS produces a cluster-scale stellar mass gradient of -0.05 log(M_*/M_sun)/Mpc. This mass segregation drives the predicted cluster-scale metallicity gradient of -0.03 dex/Mpc. However, the effects of RPS alone can not explain the higher metallicities measured in cluster galaxies at z=0.35. We hypothesize that additional mechanisms including steep internal metallicity gradients and self-enrichment due to gas strangulation are needed to reproduce our observations at z=0.35.Comment: 17 pages, 21 figures, accepted for publication Ap

    An HPSG approach to Welsh unbounded dependencies

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    Welsh is a language in which unbounded dependency constructions involve both gaps and resumptive pronouns (RPs). Gaps and RPs appear in disjoint sets of environments. Otherwise, however, they are quite similar. This suggests that they involve the same mechanism, and in HPSG that they involve the SLASH feature. It is possible to provide an analysis in which RPs are associated with the SLASH feature but are also the ordinary pronouns which they appear to be

    Brain Trust: Students for Students: VCU to RPS Mentorship Program

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    As a public, urban research institution, Virginia Commonwealth University embraces the importance of developing university-community partnerships that generate innovative solutions to societal challenges and prepare engaged citizens of tomorrow. The Students for Students: VCU to RPS Mentorship Program provides a model that will connect current VCU students to current Richmond Public Schools (RPS) students through a formal, multi-year mentorship. The ultimate goal of this program is to support and positively influence RPS students, while providing current VCU students with an opportunity to give back to the community while developing their mentorship skills. The mentoring relationship will seek to motivate RPS sophomores, juniors and seniors to improve school performance, graduate on time, and craft a post-high school path

    Differential stoichiometry among core ribosomal proteins

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    Understanding the regulation and structure of ribosomes is essential to understanding protein synthesis and its deregulation in disease. While ribosomes are believed to have a fixed stoichiometry among their core ribosomal proteins (RPs), some experiments suggest a more variable composition. Testing such variability requires direct and precise quantification of RPs. We used mass-spectrometry to directly quantify RPs across monosomes and polysomes of mouse embryonic stem cells (ESC) and budding yeast. Our data show that the stoichiometry among core RPs in wild-type yeast cells and ESC depends both on the growth conditions and on the number of ribosomes bound per mRNA. Furthermore, we find that the fitness of cells with a deleted RP-gene is inversely proportional to the enrichment of the corresponding RP in polysomes. Together, our findings support the existence of ribosomes with distinct protein composition and physiological function.Comment: 31 pages, 8 figure
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