Disease relevance of 15S

• Two distinct forms of globin messenger RNA were isolated from mouse spleen cells infected with Friend erythroleukemia virus: polyribosomal messenger ribonucleoprotein particles (15S mRNP), and their corresponding protein-free mRNAs obtained by chemical deproteinization [1].
• Selective removal of RNA-binding proteins from the ascites cell lysate did not affect globin synthesis when the mRNA was supplied as 15S mRNP; deproteinized mRNA however was not translated [1].
• Material sedimenting at 26S was translated into polypeptides corresponding to the largest virion polypeptides II to IV, a 22S fraction corresponding to polypeptide V, and smaller polypeptides and a 15S fraction corresponding to polypeptide IX [2].

High impact information on 15S

• RNA derived from the mRNP sedimented between 5S and 40S on sucrose density gradients, with the greatest radioactivity in the region of 15S [3].
• Labeled globin RNA found in the cytoplasm after a very short pulse with tritiated uridine is of the "mature" 9S size while labeled globin RNA in the nuclei is exclusively in the form of 15S precursor molecules, suggesting that cytoplasmic globin RNA is not of nuclear origin [4].
• The influence of cortisol and prolactin on casein gene expression in the mammary gland of lactating BALB/c mice was measured by using a specific cDNA probe to 15S casein mRNA (cDNAcsn) [5].
• Using the electron microscope to visualize hybrid structures formed between this gene and the purified 15S beta-globin mRNA precursor, we show that the intervening sequence is present within the larger precursor molecule [6].
• On the basis of these observations, we conclude that nucleated erythroid cells obtained from the spleens of anemic mice have a 15S RNA which contains globin mRNA sequences [7].

Biological context of 15S

• An analysis of the kinetics of hybridization of the cDNA derived from the 15S casein mRNA (cDNA12S) with their individual mRNA templates indicated that greater than 90% hybridization occurred over a R0t range of one and one-half logs with R0t 1/2 values of 0.0023 and 0.0032 mol s l.-1, respectively [8].

Anatomical context of 15S

• 15S cells never differentiated into osteoclasts [9].
• FDCP-mix cell lines A4, C2GM, and 15S were cocultured with periosteum-free 17-day-old fetal metatarsal bones [9].
• No TRBV group was uniquely expressed in significant numbers in thymocytes, although small numbers of TRBV groups 2S, 9S and 15S were only recovered from T cells [10].

Associations of 15S with chemical compounds

• Mutation of both of these amino acids to the corresponding amino acids in 15-LOX-2 (Asp and Val, respectively) converted the positional specificity from 8S to 90% 15S without yielding any other by-products [11].
• Finally, an analysis by fluorography on 5-20% (w/v) polyacrylamide gradient slab gels of the total proteins synthesized in response to both the 15S and 12S casein mRNAs revealed a close correspondence with those proteins which were specifically immunoprecipitated [12].
• First, 5-month-old mice were fed an AIN-76 diet containing either 150 g fresh soyabean oil/kg (15S), 50 g fresh soyabean oil/kg + 100 g oxidised frying oil/kg (5S10F) or 5S10F supplemented with all-rac-alpha-tocopheryl acetate at 275 mg/kg diet level (5S10F5E) or 550 mg/kg (5S10F10E), respectively, in experiment 1 [13].

Other interactions of 15S

• Presence of a putative 15S precursor to beta-globin mRNA but not to alpha-globin mRNA in Friend cells [14].
• Three size classes of virus specific poly-A containing mRNA are identified and they are 35S, 20S-25S, and 10S-15S [15].
• The in vitro resistance profile, inhibitory activities against cytochrome P450 isozymes and pharmacokinetic properties of inhibitor 15S will be discussed [16].
• 6. Saccharomyces cerevisiae mitochondrial probes including Cob, ATPase VI and IX, and cytochrome oxidase I gene sequences, 21S and 15S rRNAs, and mouse mitochondrial DNA showed no significant hybridization with any restriction fragments of Tetrahymena mitochondrial DNA [17].

Analytical, diagnostic and therapeutic context of 15S

• The 15S RNA was partially resolved from mature globin mRNA by neutral sucrose density gradient centrifugation [7].
• Immunoprecipitation and Western blot analysis of chromatographic fractions enriched in human U2 small nuclear ribonucleoprotein particles of distinct sizes (12S, 15S, and 17S), reflecting their variable association with splicing factors SF3a and SF3b, strongly suggests that the 146-kDa protein reported here is a constituent of the SF3b complex [18].
• Northern blot analysis with RNA from 21C11, an L3T4+ (CD4+-equivalent) ovalbumin-specific class II-restricted T cell line, revealed a 15S band that hybridized to this MuLT fragment [19].

References