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- Influence of Acetobacter pasteurianus SKU1108 aspS Gene Expression on Escherichia coli Morphology
- Kannipa Tasanapak , Uraiwan Masud-Tippayasak , Kazunobu Matsushita , Wichien Yongmanitchai , Gunjana Theeragool
- J. Microbiol. 2013;51(6):783-790. Published online December 19, 2013
- DOI: https://doi.org/10.1007/s12275-013-2619-6
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- 3 Crossref
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Abstract
- The aspS gene encoding Aspartyl-tRNA synthetase (AspRS) from a thermotolerant acetic acid bacterium, Acetobacter pasteurianus SKU1108, has been cloned and characterized. The open reading frame (ORF) of the aspS gene consists of 1,788 bp, encoding 595 amino acid residues. The highly conserved Gly-Val-Asp-Arg ATP binding motif (motif 3) is located at the position 537-540 in the C-terminus. Deletion analysis of the aspS gene upstream region suggested that the promoter is around 173 bp upstream from the ATG initiation codon. Interestingly, transformation with the plasmids pGEM-T138, pUC138, and pCM138 synthesizing 138 amino acid C-terminal fragments of AspRS, that carry the ATP binding domain, caused E. coli cell lengthening at 37 and 42°C. Moreover, E. coli harboring pUC595 (synthesizing all 595 amino acids) and a disordered aspS gene in pGEM-T138 had normal rod shapes. The normal rod shape was observed in E. coli harboring pD539V following site-directed mutagenesis of the ATP binding domain. We propose that overproduction of truncated C-terminal peptides of AspRS may cause sequestration of intracellular ATP in E. coli, leaving less ATP for cell division or shaping cell morphology.
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- Response of the microbiome–gut–brain axis in Drosophila to amino acid deficit
Boram Kim, Makoto I. Kanai, Yangkyun Oh, Minsoo Kyung, Eun-Kyoung Kim, In-Hwan Jang, Ji-Hoon Lee, Sang-Gyu Kim, Greg S. B. Suh, Won-Jae Lee
Nature.2021; 593(7860): 570. CrossRef - Genome-Wide Identification of Small RNAs in Bifidobacterium animalis subsp. lactis KLDS 2.0603 and Their Regulation Role in the Adaption to Gastrointestinal Environment
De-Quan Zhu, Fei Liu, Yu Sun, Li-Mei Yang, Li Xin, Xiang-Chen Meng, Yung-Fu Chang
PLOS ONE.2015; 10(2): e0117373. CrossRef - Acetic acid bacteria: A group of bacteria with versatile biotechnological applications
Natsaran Saichana, Kazunobu Matsushita, Osao Adachi, Ivo Frébort, Jitka Frebortova
Biotechnology Advances.2015; 33(6): 1260. CrossRef
- Response of the microbiome–gut–brain axis in Drosophila to amino acid deficit
- Organization of Three rRNA (rrn) Operons from Sphingobium chungbukense DJ77
- Sun-Mi Yeon , Beom-Soon Choi , Young-Chang Kim
- J. Microbiol. 2008;46(6):697-703. Published online December 24, 2008
- DOI: https://doi.org/10.1007/s12275-008-0193-0
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- 4 Scopus
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Abstract
- The nucleotide sequences of all three rRNA operons (rrnA, rrnB, and rrnC) of Sphingobium chungbukense DJ77 were determined. The three rrn operons have the same gene order (16S rRNA-tRNAIle-tRNAAla-23S rRNA-5S rRNA-tRNAfMet). The nucleotide sequences were identical over a 5,468 bp region spanning the 16S rRNA gene to the 5S rRNA gene. Variability was observed in the 5S rRNA-tRNAfMet spacer sequence of rrnB. The tRNAfMet gene sequences were identical except for two bases (T5794 and A5871 in rrnB, T5942 and A5956 in rrnA, but C5942 and G5956 in rrnC). Comparative sequence analyses of ribosomal RNA operons from DJ77 with those of the class Alphaproteobacteria, to which the genus Sphingobium belongs, reveal close evolutionary relationships with other members of the order Sphingomonadales.
- Growth Inhibition of Escherichia coli during Heterologous Expression of Bacillus subtilis Glutamyl-tRNA Synthetase that Catalyzes the Formation of Mischarged Glutamyl-tRNA_1^Gln
- Ji-Won Baick , Jang-Ho Yoon , Suk Namgoong , Dieter S?l , Sung-Il Kim
- J. Microbiol. 2004;42(2):111-116.
- DOI: https://doi.org/2036 [pii]
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Abstract
- It is known that Bacillus subtilis glutamyl-tRNA synthetase (GluRS) mischarges E. coli tRNA_1^Gln with glutamate in vitro. It has also been established that the expression of B. subtilis GluRS in Escherichia coli results in the death of the host cell. To ascertain whether E. coli growth inhibition caused by B. subtilis GluRS synthesis is a consequence of Glu-tRNA_1^ Gln formation, we constructed an in vivo test system, in which B. subtilis GluRS gene expression is controlled by IPTG. Such a system permits the investigation of factors affecting E. coli growth. Expression of E. coli glutaminyl-tRNA synthetase (GlnRS) also ameliorated growth inhibition, presumably by competitively preventing tRNA_1^Gln misacylation. However, when amounts of up to 10 mM L-glutamine, the cognate amino acid for acylation of tRNA_1^ Gln, were added to the growth medium, cell growth was unaffected. Overexpression of the B. subtilis gatCAB gene encoding GlutRNA^Gln amidotransferase (Glu-AdT) rescued cells from toxic effects caused by the formation of the mischarging GluRS. This result indicates that B. subtilis Glu-AdT recognizes the mischarged E. coli GlutRNA_1^Gln, and converts it to the cognate Gln-tRNA_1^Gln species. B. subtilis GluRS-dependent Glu-tRNA_1^Gln formation may cause growth inhibition in the transformed E. coli strain, possibly due to abnormal protein synthesis.
- Isolation and characterization of pre-tRNA^Val splicing Mutants of Schizosaccharomyces pombe
- Hwang, Ku Chan , Kim, Dae Myung
- J. Microbiol. 1997;35(4):334-340.
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Abstract
- A collection of 132 temperature sensitive (ts) mutants was generated by the chemical mutagenesis of Schizosaccharomyces pombe wild type strain and screened for tRNA splicing defects on Northern blots by hybridization with an oligonucleotide that recognizes the exon of the S. pombe tRNA^Val as a probe. We identidied 6 mutants which accumulate precursor tRNA^Val. Among them, 2 mutants exhibited remarkable morphological differences compared to wild type cells. One tRNA splicing mutant showed elongated cell shape in permissive as well as non-permissive cultures. The other mutant exhibited shortened cell morphology only in nonpermissive culture. The total RNA pattern in the splicing mutants appeared to be normal. Genetic analysis of four tRNA^Val splicing mutants demonstrated that the mutation reside in different genes.
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