Disease relevance of 16S

• Hypoxia led to a decline of Nrf1 and 16S rRNA levels also through a mechanism blocked with PK11195 [1].
• Genetic diversity on 16S rDNA sequence and phylogenic tree analysis in Pasteurella pneumotropica strains isolated from laboratory animals [2].
• First, the 16S sequence CCUCC, implicated in mRNA binding by E. coli ribosomes, is absent from each eucaryotic rRNA sequence [3].
• The 16S rRNA and flagellin in genes of Borrelia spp were sequenced by PCR and assessed by phylogenetic analyses [4].
• Two cDNA libraries were constructed, using respectively the 12S and the 16S sucrose gradient fractions of polysomal poly (A)+ RNA from mouse C243 cells induced with Newcastle disease virus [5].

High impact information on 16S

• Myotubes of a mouse muscle-cell line (C2) synthesize in culture a 16S form of acetylcholinesterase that is normally found only in regions of adult mouse muscle that contain endplates [6].
• Its extraction by high ionic strength solutions lacking detergent suggests that the 16S form is associated with the extracellular matrix by ionic interactions [6].
• Collagenase treatment, which removes only the 16S form, abolishes this staining pattern, indicating that the patches consist of the 16S enzyme [6].
• A gene for phenylalanine tRNA is located immediately adjacent to the 5' end of the 12S rRNA gene, a valine tRNA gene occupies the entire region between the 12S and 16S rRNA genes and a leucine tRNA gene is located immediately adjacent to the 3' end of the 16S gene [7].
• The microbial ecology of the digestive tracts of conventionally raised and conventionalized zebrafish was characterized by sequencing libraries of bacterial 16S rDNA amplicons [8].

Chemical compound and disease context of 16S

• Following agarose gel electrophoresis, the fragments were subjected to Southern blot hybridization with a digoxigenin-labeled cDNA probe transcribed from Escherichia coli 16S and 23S rRNA [9].
• The mtDNA 16S rRNA chloramphenicol (CAP) resistance mutation was introduced into the mouse female germline and caused cataracts and rod and cone abnormalities in chimeras and neonatal lethal myopathy and cardiomyopathy in mutant animals [10].
• METHODS: Chlamydia pneumoniae membrane protein, heat shock protein 60, and lipopolysaccharide were detected by immunocytochemistry, and genomic DNA and 16S rRNA by in situ hybridisation in paraffin wax embedded sections of cultured HEp2 cells infected with C pneumoniae and of lungs from mice infected intranasally with C pneumoniae [11].

Biological context of 16S

• In intact cells, the active site of the 16S acetylcholinesterase is protected by a membrane-impermeable inhibitor, and this form of the enzyme can be removed by treatment of the cells with collagenase [6].
• Although initial phenotypic and 16S rRNA analysis identified this isolate as B. cereus, the rapid generation and analysis of a high-coverage draft genome sequence revealed the presence of a circular plasmid, named pBCXO1, with 99.6% similarity with the B. anthracis toxin-encoding plasmid, pXO1 [12].
• Although these trees are phenograms, they carry with them strong phylogenetic signatures and are remarkably similar to 16S-like rRNA-based phylogenies [13].
• Negative dominance of m53DD on 16S rRNA expression and CMXRos staining, and rescue of these parameters with PK11195, imply a direct positive effect of p53 on mitochondrial biogenesis and function [14].
• A 16S RNA species containing gamma-globin mRNA sequences was identified by hybridisation to 32P-labelled human gamma-globin cDNA recombinant plasmid pHgamma GI [15].

Anatomical context of 16S

• Thus, the 16S, or endplate form of AChE is not specifically regulated by electrical or contractile activity in the C2 cell line [16].
• Developmental regulation of 16S acetylcholinesterase and acetylcholine receptors in a mouse muscle cell line [16].
• We conclude that the 16S enzyme in C2 myotubes occurs in focal patches on the cell surface, where it is associated with the extracellular matrix [6].
• It may mean that at least some of the basal lamina-embedded 16S AcChoEase is preassembled intracellularly in the sarcoplasmic reticulum [17].
• However, in the A fraction, most of the 16S AcChoEase found is solubilized by detergent alone, suggesting an association with microsomal membranes [17].

Associations of 16S with chemical compounds

• Total cellular polyadenylated Py-specific RNA molecules having an S value in the range of 16S to 20S were purified by oligodeoxythymidylic acidcellulose column chromatography, preparative hybridization with Py DNA, and sucrose gradient centrifugation [18].
• Role of a 16S glycoprotein complex in cellular adhesion [19].
• Whole-cell extracts prepared from mercuric chloride-treated cells or from cell extracts treated in vitro failed to support in vitro transcription of 16S rRNAp and lacSp promoters [20].
• The chemical half-lives of the 16S rRNA precursors in the methionine-starved rickettsiae did not differ significantly from those in the normal rickettsiae [21].
• In addition, there was a reduction in the expression of cntB compared to the expression of the 16S rRNA gene at higher sodium nitrite concentrations [22].

Regulatory relationships of 16S

• The time course of recovery of the molecular forms in the diaphragm occurred rather quickly with the smaller 4S and 10S forms recovering to control levels faster than the larger 16S form [23].
• One cDNA clone was found to correspond to mitochondrial 16S rRNA and a second was identified as the murine equivalent of previously described cDNA clones for the hamster 78-kDa glucose-regulated protein (GRP78) and the rat immunoglobulin heavy-chain-binding protein [24].
• Collagenase-induced alteration in mouse 16S acetylcholinesterase [25].

Other interactions of 16S

• These functional relationships suggest that Bzrp-dependent signals regulate the Nrf1 --> Tfam1 --> mtDNA --> 16S rRNA pathway in response to oxygen levels [1].
• According to phenotypic reactions and 16S rDNA sequencing, the isolates were most similar to biotype Heyl [26].
• The 4-6S and 10S forms appeared 1 day after the cells began to fuse, whereas the 16S form appeared only 2 days after fusion began [16].
• About one-third of the clones analyzed from 16S rDNA libraries of interleukin-2-deficient mice represented Enterobacteriaceae, whereas none of the clones analyzed from the healthy controls harbored 16S rDNA from Enterobacteriaceae [27].
• Thus, electrical membrane activity, and not contraction per se, is directly involved in the regulation of levels of specific activity of and accumulation of the asymmetric (16S) form of AChE in muscle cells in culture [28].

Analytical, diagnostic and therapeutic context of 16S

• To reveal the genetic diversity of Pasteurella pneumotropica, the 16S rDNA sequence and multiple alignments were performed for 35 strains (from 17 mice, 13 rats, 3 hamsters, 1 rabbit, and 1 guinea pig) identified as P. pneumotropica using a commercial biochemical test kit or PCR test and two reference strains (ATCC 35149 and CNP160) [2].
• The 16S form was detected only in nerve-muscle cocultures [29].
• In situ hybridization for H. hepaticus 16S rRNA showed that the bacteria was found throughout the liver associated with hepatitis but not within tumors [30].
• During late lytic infection of mouse kidney cell cultures polyoma 16S and 19S (late 19S RNA) were isolated by oligo(dT)-cellulose chromatography [31].
• In a recent case of scrub typhus in Australia, Orientia tsutsugamushi isolated from the patient's blood was tested by sequence analysis of the 16S rDNA gene [32].

References