The nucleotide sequences of two tryptophane-tRNAs from brewer's yeast

The study entitled “Observance of PMC and Its Relation to the Presence of Three Levels of Politeness” investigates politeness realizations according to Principles of Mutual Consideration (PMC) between two different cultures and its relation to the presence of three levels of politeness: pre-event, on-the-spot, and post-event politeness as proposed by Aziz (2000). PMC works as a cause and effect logic wgich consists of four sub-principles: i.e. harm and favor potential, shared-feeling, prima-facie, and continuity principles. The main data of the study were retrieved from www.rcti.tv on 26th April, 2010 which contained the opening-part of an interview script between an Indonesian Journalist and the President of the Unites States. Using the PMC framework, the study found that there is balanced-order in observing PMC’s sub-principles. This is due to the fact that both the interviewer and the interviewee had the intention to favour one another. This was realized in their complete observance of four PMC’s sub-principles. The study concluded that the observance of PMC together with its three levels of politeness is mainly motivated to balance and create harmony.Keywords: Principle of Mutual Consideration (PMC), Three Levels of Politeness

Isolation of Bacillus spp. from Thai fermented soybean (Thua-nao): screening for aflatoxin B1 and ochratoxin A detoxification.

Aims: To study the interaction between Bacillus spp. and contaminating Aspergillus flavus isolated strains from Thai fermented soybean in order to limit aflatoxin production. To study the detoxification of aflatoxin B1 (AFB1) and ochratoxin A (OTA) by Bacillus spp. in order to find an efficient strain to remove these toxins. Methods and Results: One A. flavus aflatoxin-producing strain and 23 isolates of Bacillus spp. were isolated from soybean and fresh Thua-nao collected from the north of Thailand. Inhibition studies of A. flavus and A. westerdijkiae NRRL 3174 (reference strain) growth by all isolates of Bacillus spp. were conducted by dual culture technique on agar plates. These isolates were also tested for AFB1 and OTA detoxification ability on both solid and liquid media. Most of the strains were able to detoxify aflatoxin but only some of them could detoxify OTA. Conclusions: One Bacillus strain was able to inhibit growth of both Aspergillus strains and to remove both mycotoxins (decrease of 74% of AFB1 and 92·5% of OTA). It was identified by ITS sequencing as Bacillus licheniformis. The OTA decrease was due to degradation in OTα. Another Bacillus strain inhibiting both Aspergillus growth and detoxifying 85% of AFB1 was identified as B. subtilis. AFB1 decrease has not been correlated to appearance of a degradation product. Significance and Impact of the Study: The possibility to reduce AFB1 level by a strain from the natural flora is of great interest for the control of the quality of fermented soybean. Moreover, the same strain could be a source of efficient enzyme for OTA degradation in other food or feeds

Isolation and characterization of the gene coding for Escherichia coli arginyl-tRNA synthetase.

The gene coding for Escherichia coli arginyl-tRNA synthetase (argS) was isolated as a fragment of 2.4 kb after analysis and subcloning of recombinant plasmids from the Clarke and Carbon library. The clone bearing the gene overproduces arginyl-tRNA synthetase by a factor 100. This means that the enzyme represents more than 20% of the cellular total protein content. Sequencing revealed that the fragment contains a unique open reading frame of 1734 bp flanked at its 5' and 3' ends respectively by 247 bp and 397 bp. The length of the corresponding protein (577 aa) is well consistent with earlier Mr determination (about 70 kd). Primer extension analysis of the ArgRS mRNA by reverse transcriptase, located its 5' end respectively at 8 and 30 nucleotides downstream of a TATA and a TTGAC like element (CTGAC) and 60 nucleotides upstream of the unusual translation initiation codon GUG; nuclease S1 analysis located the 3'-end at 48 bp downstream of the translation termination codon. argS has a codon usage pattern typical for highly expressed E. coli genes. With the exception of the presence of a HVGH sequence similar to the HIGH consensus element, ArgRS has no relevant sequence homologies with other aminoacyl-tRNA synthetases

Aspartyl-tRNA synthetase from Escherichia coli: cloning and characterisation of the gene, homologies of its translated amino acid sequence with asparaginyl- and lysyl-tRNA synthetases.

By screening of an Escherichia coli plasmidic library using antibodies against aspartyl-tRNA synthetase (AspRS) several clones were obtained containing aspS, the gene coding for AspRS. We report here the nucleotide sequence of aspS and the corresponding primary structure of the aspartyl-tRNA synthetase, a protein of 590 amino acid residues with a Mr 65,913, a value in close agreement with that observed for the purified protein. Primer extension analysis of the aspS mRNA using reverse transcriptase located its 5'-end at 94 nucleotides upstream of the translation initiation AUG; nuclease S1 analysis located the 3'-end at 126 nucleotides downstream of the stop codon UGA. Comparison of the DNA-derived protein sequence with known aminoacyl-tRNA sequences revealed important homologies with asparaginyl- and lysyl-tRNA synthetases from E.coli; more than 25% of their amino acid residues are identical, the homologies being distributed preferencially in the first part and the carboxy-terminal end of the molecule. Mutagenesis directed towards a consensus tetrapeptide (Gly-Leu-Asp-Arg) and the carboxy-terminal end showed that both domains could be implicated in catalysis as well as in ATP binding