Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Escherichia coli selenophosphate synthetase (SPS, the selD gene product) catalyzes the production of monoselenophosphate, the selenium donor compound required for synthesis of selenocysteine (Sec) and seleno-tRNAs. We report the molecular cloning of human and mouse homologs of the selD gene, designated Sps2, which contains an in-frame TGA codon at a site corresponding to the enzyme's putative active site. These sequences allow the identification of selD gene homologs in the genomes of the bacterium Haemophilus influenzae and the archaeon Methanococcus jannaschii, which had been previously misinterpreted due to their in-frame TGA codon. Sps2 mRNA levels are elevated in organs previously implicated in the synthesis of selenoproteins and in active sites of blood cell development. In addition, we show that Sps2 mRNA is up-regulated upon activation of T lymphocytes and have mapped the Sps2 gene to mouse chromosome 7. Using the mouse gene isolated from the hematopoietic cell line FDCPmixA4, we devised a construct for protein expression that results in the insertion of a FLAG tag sequence at the N terminus of the SPS2 protein. This strategy allowed us to document the readthrough of the in-frame TGA codon and the incorporation of 75Se into SPS2. These results suggest the existence of an autoregulatory mechanism involving the incorporation of Sec into SPS2 that might be relevant to blood cell biology. This mechanism is likely to have been present in ancient life forms and conserved in a variety of living organisms from all domains of life.
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PMID:Identification of a novel selD homolog from eukaryotes, bacteria, and archaea: is there an autoregulatory mechanism in selenocysteine metabolism? 898 68

In bacteria, synonymous codon usage can be considerably affected by base composition at neighboring sites. Such context-dependent biases may be caused by either selection against specific nucleotide motifs or context-dependent mutation biases. Here we consider the evolutionary conservation of context-dependent codon bias across 11 completely sequenced bacterial genomes. In particular, we focus on two contextual biases previously identified in Escherichia coli; the avoidance of out-of-frame stop codons and AGG motifs. By identifying homologues of E. coli genes, we also investigate the effect of gene expression level in Haemophilus influenzae and Mycoplasma genitalium. We find that while context-dependent codon biases are widespread in bacteria, few are conserved across all species considered. Avoidance of out-of-frame stop codons does not apply to all stop codons or amino acids in E. coli, does not hold for different species, does not increase with gene expression level, and is not relaxed in Mycoplasma spp., in which the canonical stop codon, TGA, is recognized as tryptophan. Avoidance of AGG motifs shows some evolutionary conservation and increases with gene expression level in E. coli, suggestive of the action of selection, but the cause of the bias differs between species. These results demonstrate that strong context-dependent forces, both selective and mutational, operate on synonymous codon usage but that these differ considerably between genomes.
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PMID:Evolutionary lability of context-dependent codon bias in bacteria. 1075 70

We have previously reported on cloning a DNA repair gene designated as uvr3 by virtue of its ability to phenotypically complement the UV sensitivity of mutant strain MBH3. Subsequently, we identified the uvr3 gene to be the uvrA gene (gene identification number HI0249) of Haemophilus influenzae Rd. The uvrA gene is a component of the UvrABC excision repair pathway. We studied molecular basis of the UV sensitivity of the MBH3 strain and identified a G-->A transition at nucleotide position 2700 of the uvrA gene, altering the Trp-900 codon (TGG) to a nonsense codon (TGA). Thus, the UvrA protein produced in the mutant strain MBH3 is likely to be truncated and unable to carry out the UV-induced DNA repair, thereby rendering the strain UV sensitive.
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PMID:Molecular basis of UV-sensitive mutant strain MBH3 of Haemophilus influenzae Rd: identification of mutation in the uvrA gene. 1121 3

Thiamphenicol-glycinate-acetylcysteinate (TGA; CAS 20192-91-0) is widely used for the treatment of infections of varied aetiology. The aim of this study was to compare the antibacterial activity of thiamphenicol-glycinate (TG; CAS 15318-45-3), TGA, amoxicillin (CAS 61336-70-7) plus clavulanic acid (CAS 58001-44-8), azithromycin (CAS 83905-01-5) and ceftriaxone (CAS 104376-79-6). Minimum inhibitory concentrations (MICs) and minimum bactericidal concentrations (MBCs) were determined against Staphylococcus aureus, Klebsiella pneumoniae, Streptococcus pyogenes, Streptococcus pneumoniae, Moraxella catarrhalis and Haemophilus influenzae according to the National Committee for Clinical Laboratory Standards (NCCLS) methods. The effects of changes in assay conditions were also examined. The activity of TG and TGA was similar to that of amoxicillin plus clavulanic acid, with the exception of methicillin resistant S. aureus. Azithromycin and ceftriaxone were characterised by a limited activity against gram-positive cocci and methicillin resistant and cefinase-positive S. aureus, respectively. TG and TGA are characterized by a wide spectrum of activity, comparable to that of recent commercialized antibiotics for treatment of respiratory tract infections.
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PMID:Comparative in vitro activity of thiamphenicol-glycinate and thiamphenicol-glycinate-acetylcysteinate and other antimicrobials against respiratory pathogens. 1136 73