Disease relevance of RNU3P3

• The gene encoding the U3 SnRNA is transcriptionally induced early in infection with herpes simplex virus (HSV) [1].
• Unlike the three U3 RNA's of Novikoff hepatoma cells, U3 RNA from human tissues appears to be only one species [2].
• The RNA templates utilized were the actual HIV sequences involved in the first template switch, namely a primer binding sequence (PBS)/U5/R RNA donor template and a R/U3 RNA acceptor template [3].
• The U3-U7 gene cluster of human herpesvirus 6 (HHV-6) was replaced with an enhanced green fluorescent protein-puromycin gene cassette containing the cytomegalovirus major immediate-early promoter [4].
• Thus, an independently expressed selectable marker gene flanked by a loxP target sequence was cloned into the U3 region of a Moloney murine leukemia virus vector [5].

High impact information on RNU3P3

• Here we report that three pseudogenes (U1.101, U2.13 and U3.5) are flanked by perfect short direct repeats of 16 to 19 base pairs [6].
• U3 small nuclear RNA is hydrogen-bonded to high molecular weight nucleolar RNA and can be isolated from greater than 60S pre-ribosomal ribonucleoprotein particles, suggesting that it is involved in processing of ribosomal RNA precursors (pre-rRNA) or in ribosome biogenesis [7].
• Here we report the purification of U3 snoRNP from CHO cells using anti-m3G-immunoaffinity and mono Q anion-exchange chromatography [8].
• Using a rabbit antiserum raised against the 55 kDa protein, and an in vitro reconstitution assay, we have localised the 55 kDa protein binding site on the U3 snoRNA [8].
• The strategy exploited (i) the natural life cycle of retroviruses, involving duplication of terminal control regions U5 and U3 to generate long terminal repeats (LTRs) and (ii) the ability of the P1 phage site-specific recombinase (Cre) to excise any sequences positioned between two loxP target sequences from the mammalian genome [5].

Chemical compound and disease context of RNU3P3

• Tris(hydroxymethyl)aminomethane (Tris) (10 mM, pH 7.0) extracts of Novikoff hepatoma nucleoli, which contained about 80% of total nucleolar U3 RNA, were analyzed by sucrose density gradient centrifugation [9].

Biological context of RNU3P3

• We previously demonstrated that pseudogenes complementary to the small nuclear RNAs U1, U2 and U3 are dispersed and abundant in the human genome [6].

Anatomical context of RNU3P3

• In eukaryotic cells, the gamma-monomethylphosphate cap structure has been identified in four small RNAs, namely, U6, 7SK, B2, and plant U3 RNAs [10].
• Localization of U3 RNA molecules in nucleoli of HeLa and mouse 3T3 cells by high resolution in situ hybridization [11].
• In this study we report the detection of autoantibodies to the nucleolar U3- and Th(7-2) ribonucleoprotein (RNP) particles in sera from patients with connective tissue diseases [12].
• The method described employs radioactively labelled antisense U3- and Th RNA which are hybridized to immunoprecipitated U3- or Th RNA from a HeLa cell extract [12].

Associations of RNU3P3 with chemical compounds

• By immunofluorescence testing using antibodies raised to a fusion protein of MBP (maltose-binding protein) and U3, the U3 viral antigen was detected as early as 24 h p.i. in HHV-6A-infected U373 cells [13].

Analytical, diagnostic and therapeutic context of RNU3P3

• Western blotting further confirmed its reactivity with this scleroderma-related U3 RNP protein [14].
• Six transcripts with different molecular weights of 7.5-1.8 kb were detected by Northern blot analysis using a U3-specific probe [13].
• Sequence analyses of the respective cDNA clones and primer extension experiments revealed that the U3 gene encoded the 2.0- and 3.5-kb transcripts and had no splicing within the U3 gene region [13].

References