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Biosci Biotechnol Biochem [journal]
- MurA as a primary target of tulipalin B and 6-tuliposide B. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2517-9.
(-)-Tulipalin B and (+)-6-tuliposide B were confirmed to inhibit MurA in vitro. However, contrary to fosfomycin, these compounds showed potent inhibitory activities against MurA overexpressing Escherichia coli, especially in the presence of UDP-GlcNAc. These observations suggest that these compounds induced bacterial cell death not through a MurA malfunction, but in such a MurA-mediated indirect manner as the inhibition of other Mur enzymes.
- Mutations in the CCD4 carotenoid cleavage dioxygenase gene of yellow-flesh peaches. [Journal Article]
- Biosci Biotechnol Biochem 2013; 77(12):2514-6.
Peach trees bear either white- or yellow-flesh fruit. We found that Japanese peach cultivars have two types of mutation in a carotenoid catabolic gene, CCD4: the insertion of a retrotransposon, and a frame shift in the microsatellite sequences of the first exon. CCD4 in yellow-flesh peaches was disrupted by these mutations.
- Lysophosphatidylcholine potentiates BDNF-induced TrkB phosphorylation and downstream signals in cerebellar granule neurons. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2510-3.
We found that brain-derived neurotrophic factor (BDNF)-induced phosphorylation of mitogen-activated protein kinase (MAPK) and Akt in cerebellar granule neurons was specifically potentiated by LPC. LPC also augmented the BDNF-induced phosphorylation of TrkB, the receptor for BDNF. In TrkB-transfected CHO-K1 cells, LPC potentiated BDNF-induced MAPK phosphorylation. These results suggest that LPC plays a role in BDNF-TrkB signaling by regulating the activation of TrkB.
- Isolation of a non-urea-producing sake yeast strain carrying a discriminable molecular marker. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2505-9.
In the fermentation industry, the traceability of microorganisms during the process is important to ensure safety and efficacy. Ethyl carbamate, a group-2A carcinogen, is produced from ethanol and urea during the storage of food/alcoholic beverages. We isolated non-urea-producing sake yeast car1 mutants carrying a discriminable molecular marker, and demonstrated, by the use of PCR assays, that these mutants are useful for traceability analysis and identification during the sake brewing process.
- A secondary structure in the 5' untranslated region of adhE mRNA required for RNase G-dependent regulation. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2473-9.
Escherichia coli RNase G is involved in the degradation of several mRNAs, including adhE and eno, which encode alcohol dehydrogenase and enolase respectively. Previous research indicates that the 5' untranslated region (5'-UTR) of adhE mRNA gives RNase G-dependency to lacZ mRNA when tagged at the 5'-end, but it has not been elucidated yet how RNase G recognizes adhE mRNA. Primer extension analysis revealed that RNase G cleaved a phosphodiester bond between -19A and -18C in the 5'-UTR (the A of the start codon was defined as +1). Site-directed mutagenesis indicated that RNase G did not recognize the nucleotides at -19 and -18. Random deletion analysis indicated that the sequence from -145 to -125 was required for RNase G-dependent degradation. Secondary structure prediction and further site-directed deletion suggested that the stem-loop structure, with a bubble in the stem, is required for RNaseG-dependent degradation of adhE mRNA.
- Heterologous production of desferrioxamines with a fusion biosynthetic gene cluster. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2467-72.
Desferrioxamines E (1), D2 (2), X1 (3), and X2 (4), four macrocyclic N-hydroxy-N-succinyl diamine-based siderophores, were produced efficiently by heterologous expression of a fusion biosynthetic gene cluster. This expression system consisted of three genes (mbsA-C) from marine metagenomic DNA and one gene (dfoC(C)) from the terrestrial bacterium Erwinia amylovora. The first three genes are functional in the production of the common monomers N-hydroxy-N-succinyl cadaverine (5, HSC) and N-hydroxy-N-succinyl putrescine (6, HSP), whereas dfoC(C) catalyzes the oligomerization and the macrocyclization reactions of compounds 5 and 6 to form compounds 1-4. This fusion gene cluster system provides a convenient expression platform for various biosynthetic genes of HSC-HSP based siderophores by simply switching the fourth gene by the cassette process.
- Identification and characterization of a gene encoding an ABC transporter expressed in the dicarboxylic acid-producing yeast Candida maltosa. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2502-4.
A gene, CmCDR1, encoding an ABC transporter of the dicarboxylic acid (DCA)-producing yeast Candida maltosa was cloned. Transcription of CmCDR1 was upregulated in a DCA-hyper-producing mutant of C. maltosa in a later phase of culture on n-dodecane, but not in its parental strain. CmCDR1 expression was significantly induced by the longer-chain DCA in this mutant.
- Deciphering the roles of glycan processing in glycoprotein quality control through organic synthesis. [Journal Article]
- Biosci Biotechnol Biochem 2013; 77(12):2331-8.
Protein quality control (QC) in the endoplasmic reticulum (ER) comprises many aspects, including folding and transport of nascent proteins and degradation of misfolded proteins. Recent studies have revealed that high-mannose-type glycans play pivotal roles in the QC process. To gain knowledge of the molecular basis of this process with well-defined homogeneous compounds, we achieved a convergent synthesis of high-mannose-type glycans and their functionalized derivatives. A major part of our study focused on analyses of UDP-Glc: glycoprotein glucosyltransferase (UGGT) and ER glucosidase II, which play crucial roles in glycoprotein QC, to clarify their specificities. In addition, we established an in vitro assay system mimicking the in vivo condition, which is highly crowded due to the presence of various macromolecules.
- Protease-deficient Saccharomyces cerevisiae strains for the synthesis of human-compatible glycoproteins. [Journal Article, Research Support, Non-U.S. Gov't]
- Biosci Biotechnol Biochem 2013; 77(12):2461-6.
Saccharomyces cerevisiae strains engineered previously to produce proteins with mammalian high mannose structures showed severe growth defects and decreased protein productivity. In strain YAB101, derived from one of these strains by a mutagenesis technique based on the disparity theory of evolution, these undesirable phenotypes were alleviated. Here we describe further engineering of YAB101 with the aim of synthesizing heterologous glycoproteins with Man5GlcNAc2, an intermediate for the mammalian hybrid and complex type oligosaccharides. About 60% conversion of Man8GlcNAc2 to Man5GlcNAc2 was observed after integration of Aspergillus saitoi α-1,2-mannosidase fused to the transmembrane domain of S. cerevisiae Och1. To obtain a higher yield of the target protein, a protease-deficient version of this strain was generated by disruption of PEP4 and PRB1, resulting in YAB101-4. Inactivation of these vacuolar proteases enhanced the secretion of human interferon-β by approximately 10-fold.
- Expression and characterization of a thermostable acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis involved in the degradation of insoluble cellulose acetate. [Journal Article]
- Biosci Biotechnol Biochem 2013; 77(12):2495-8.
A thermostable acetylxylan esterase gene, TTE0866, which catalyzes the deacetylation of cellulose acetate, was cloned from the genome of Caldanaerobacter subterraneus subsp. tengcongensis. The pH and temperature optima were 8.0 and 60 °C. The esterase was inhibited by phenylmethylsulfonyl fluoride. A mixture of the esterase and cellulolytic enzymes efficiently degraded insoluble cellulose acetate with a higher degree of substitution.