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Gene Review

16S  -  DNA segment, 16S

Mus musculus

 
 
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Disease relevance of 16S

 

High impact information on 16S

 

Chemical compound and disease context of 16S

 

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

References

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  14. Direct influence of the p53 tumor suppressor on mitochondrial biogenesis and function. Donahue, R.J., Razmara, M., Hoek, J.B., Knudsen, T.B. FASEB J. (2001) [Pubmed]
  15. A nuclear precursor to human gamma-globin messenger RNA. Courtney, M., Williamson, R. Nucleic Acids Res. (1979) [Pubmed]
  16. Developmental regulation of 16S acetylcholinesterase and acetylcholine receptors in a mouse muscle cell line. Inestrosa, N.C., Miller, J.B., Silberstein, L., Ziskind-Conhaim, L., Hall, Z.W. Exp. Cell Res. (1983) [Pubmed]
  17. Acetylcholinesterase of mammalian neuromuscular junctions: presence of tailed asymmetric acetylcholinesterase in synaptic basal lamina and sarcolemma. Dreyfus, P.A., Rieger, F., Pinçon-Raymond, M. Proc. Natl. Acad. Sci. U.S.A. (1983) [Pubmed]
  18. Electron microscopic mapping of RNA transcribed from the late region of polyoma virus DNA. Manor, H., Wu, M., Baran, N., Davidson, N. J. Virol. (1979) [Pubmed]
  19. Role of a 16S glycoprotein complex in cellular adhesion. Schubert, D., LaCorbiere, M. Proc. Natl. Acad. Sci. U.S.A. (1980) [Pubmed]
  20. Mercury inactivates transcription and the generalized transcription factor TFB in the archaeon Sulfolobus solfataricus. Dixit, V., Bini, E., Drozda, M., Blum, P. Antimicrob. Agents Chemother. (2004) [Pubmed]
  21. Transcriptional analysis of the 16s rRNA gene in Rickettsia prowazekii. Pang, H., Winkler, H.H. J. Bacteriol. (1996) [Pubmed]
  22. Relative neurotoxin gene expression in clostridium botulinum type B, determined using quantitative reverse transcription-PCR. Lövenklev, M., Holst, E., Borch, E., Rådström, P. Appl. Environ. Microbiol. (2004) [Pubmed]
  23. Soman and sarin inhibition of molecular forms of acetylcholinesterase in mice. Time course of recovery and reactivation by the oxime HI-6. Clement, J.G., Rosario, S., Bessette, E., Erhardt, N. Biochem. Pharmacol. (1991) [Pubmed]
  24. Differential screening of a cDNA library with cDNA probes amplified in a heterologous host: isolation of murine GRP78 (BiP) and other serum-regulated low-abundance mRNAs. Parfett, C.L., Hofbauer, R., Brudzynski, K., Edwards, D.R., Denhardt, D.T. Gene (1989) [Pubmed]
  25. Collagenase-induced alteration in mouse 16S acetylcholinesterase. Rieger, F., Ruberg, M., Shelanski, M.L. Brain Res. (1979) [Pubmed]
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