Search

mRNA stability is elaborately regulated by elements in the mRNA transcripts and their cognate RNA-binding proteins, which play important roles in regulating gene expression at the post-transcriptional level in eukaryotes. Poly(U)-binding protein 1 (Pub1), which is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae, is involved in the regulation of mRNA turnover as a trans-acting factor. It binds to transcripts containing the AU-rich element in order to protect them from degradation. Pub1 contains three RNA-recognition motifs (RRMs) which play significant roles in mRNA binding at AU-rich elements and stabilizer elements. In this study, the second RRM of Pub1 was crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 4000 as a precipitant at 283 K. An X-ray diffraction data set was collected using a single flash-cooled crystal that belonged to space group H3. [ABSTRACT FROM AUTHOR]

Cui, Y., 2019. Quality evaluation of marine statistical data on the basis of clustering algorithms. In: Li, L.; Wan, X.; and Huang, X. (eds.), Recent Developments in Practices and Research on Coastal Regions: Transportation, Environment and Economy. Journal of Coastal Research, Special Issue No. 98, pp. 151–154. Coconut Creek (Florida), ISSN 0749-0208. The quality of marine statistical data is the life of marine statistical work, and it is the key to reflecting the level of marine statistical work, which is related to the credibility of marine statistical departments. Therefore, in marine statistics work, we need to establish perfect marine statistical data quality evaluation criteria. Only by meeting the basic standards will we gradually establish a comprehensive and systematic marine statistical data quality monitoring system, which will guarantee the authority of the marine statistical data. This paper further improves the quality of marine statistical data in China by using a clustering algorithm. [ABSTRACT FROM AUTHOR]

Abstract: Yeast poly(U)-binding protein (Pub1) is a major nuclear and cytoplasmic protein that contains three RNA recognition motif (RRM) domains (termed Pub1RRM1, Pub1RRM2 and Pub1RRM3). Pub1 has been implicated as a regulator of cellular mRNA decay. Nearly 10% of all yeast mRNA decay occurs in a Pub1-dependent manner. Pub1 binds to and stabilizes AU-rich element (ARE) and ARE-like sequence-containing transcripts by protecting them from degradation through the deadenylation-dependent pathway, and also binds to and stabilizes stabilizer element (STE)-containing transcripts by preventing their degradation via the nonsense-mediated decay (NMD) pathway. RNA-binding analyses showed that Pub1 binds to poly(U) in vitro. Here we show the crystal structures of Pub1RRM2 and the first two tandem RRM domains (Pub1RRM12). Crystallography showed that the structure of Pub1RRM12 is a domain-swapped dimer. Size exclusion chromatography assay and analytical ultracentrifugation (AUC) showed that Pub1RRM12 is a monomer in solution. Kinetic analysis showed that all three individual RRM domains can bind to poly(U) with similar affinities and Pub1RRM12 binds to a long poly(U) segment with higher affinity. Mutagenesis analysis revealed that residues on the β-sheets of Pub1RRM1 and Pub1RRM2 are critical for poly(U) binding. [ABSTRACT FROM AUTHOR]