Journal of general microbiology最新文献_第8页

Cloning and sequencing of a gene encoding acidophilic amylase from Bacillus acidocaldarius. 嗜酸芽孢杆菌嗜酸淀粉酶基因的克隆与序列分析。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2399

T T Koivula, H Hemilä, R Pakkanen, M Sibakov, I Palva

{"title":"Cloning and sequencing of a gene encoding acidophilic amylase from Bacillus acidocaldarius.","authors":"T T Koivula, H Hemilä, R Pakkanen, M Sibakov, I Palva","doi":"10.1099/00221287-139-10-2399","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2399","url":null,"abstract":"Two starch-degrading enzymes produced by Bacillus acidocaldarius (renamed as Alicyclobacillus acidocaldarius) were identified. According to SDS-PAGE, the apparent molecular masses of the enzymes were 90 and 160 kDa. Eight peptide fragments and the N-terminal end of the 90 kDa polypeptide were sequenced. An oligonucleotide, based on the amino acid sequence of a peptide fragment of the 90 kDa protein, was used to screen a lambda gt10 bank of B. acidocaldarius, and the region encoding the 90 kDa protein was cloned. Unexpectedly, the ORF continued upstream of the N terminus of the 90 kDa protein. The entire ORF was 1301 amino acids (aa) long (calculated molecular mass 140 kDa) and it was preceded by a putative ribosomal binding site and a promoter. Computer analysis showed that the 1301 aa protein was closely related to an alpha-amylase-pullulanase of Clostridium thermohydrosulfuricum. We suggest that the starch-degrading 160 kDa protein of B. acidocaldarius is an alpha-amylase-pullulanase, and the 90 kDa protein is a cleavage product of the 160 kDa protein. Another ORF, apparently in the same transcription unit, was found downstream from the amylase gene. It encoded a protein that was closely related to the maltose-binding protein of Escherichia coli.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2399-407"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-10-2399","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19242137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 30

Protection by sterols against the cytotoxicity of syringomycin in the yeast Saccharomyces cerevisiae. 甾醇对紫霉素对酵母细胞毒性的保护作用。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2323

C Julmanop, Y Takano, J Y Takemoto, T Miyakawa

引用次数: 27

Formation of melanin pigment by a mutant of Bacillus thuringiensis H-14. 苏云金芽孢杆菌H-14突变体黑色素的形成。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2365

S L Hoti, K Balaraman

引用次数: 56

The temperate phages RP2 and RP3 of Streptomyces rimosus. 链霉菌的温带噬菌体RP2和RP3。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2517

H Rausch, M Vesligaj, D Pocta, G Biuković, J Pigac, J Cullum, H Schmieger, D Hranueli

{"title":"The temperate phages RP2 and RP3 of Streptomyces rimosus.","authors":"H Rausch, M Vesligaj, D Pocta, G Biuković, J Pigac, J Cullum, H Schmieger, D Hranueli","doi":"10.1099/00221287-139-10-2517","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2517","url":null,"abstract":"The oxytetracycline-producing Streptomyces rimosus strains R6-65 and R7 (ATCC 10970) are lysogenic for the two narrow-host-range phages RP2 and RP3. Both phages are released at low frequency from the lysogenic strains and form plaques on 'cured' S. rimosus strains. RP2 and RP3 are of similar shape with flexible tails and contain double-stranded DNA of about 70% G+C with cohesive ends (group B1 of bacteriophage classification). The two phages also have identical, very slow, growth kinetics in S. rimosus, with a latent phase of about 6 h and a rise period of about 4 h. RP2 and RP3 are heteroimmune and they differ slightly in their size of phage particles and length of DNA (64.7 and 62.4 kb for RP2 and RP3, respectively). The restriction maps of the two phages are completely different, and hybridization experiments showed only one short region of sequence similarity (less than 430 bp); the two phages are thus essentially unrelated. Both phages lysogenize their hosts by recombination via defined attachment (att) sites. The positions of the attP sites have been localized on the restriction maps of RP2 and RP3 to restriction fragments of 800 and 300 bp, respectively. The prophages did not affect the level of oxytetracycline production or the genetic instability of this trait.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2517-24"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-10-2517","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19243209","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 6

Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans. 变形链球菌诱导的两种不同的NADH氧化酶，分别对应于h2o2形成氧化酶和h2o形成氧化酶。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2343

M Higuchi, M Shimada, Y Yamamoto, T Hayashi, T Koga, Y Kamio

{"title":"Identification of two distinct NADH oxidases corresponding to H2O2-forming oxidase and H2O-forming oxidase induced in Streptococcus mutans.","authors":"M Higuchi, M Shimada, Y Yamamoto, T Hayashi, T Koga, Y Kamio","doi":"10.1099/00221287-139-10-2343","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2343","url":null,"abstract":"Two distinct NADH oxidases, corresponding to H2O2-forming and H2O-forming enzymes were purified to homogeneity from Streptococcus mutans and their basic properties determined. The H2O2-forming enzyme was a tetramer with a subunit molecular mass of about 56 kDa and required flavin adenine dinucleotide (FAD) for full activity. The enzyme had an isoelectric point of 6.6 and exhibited optimal activity at pH 6.0. The H2O-forming enzyme was a monomer with a molecular mass of 50 kDa and activity independent of exogenously added flavin. The enzyme had an isoelectric point of 4.8 and exhibited optimal activity between pH 7.0 and 7.5. Both enzymes oxidized NADH (Km 0.05 and 0.025 mM for the H2O2- and H2O-forming enzyme, respectively) but not NADPH and contained 1 mol of FAD per monomer. Spectra of the oxidized enzymes exhibited maxima at 271, 383 and 449 nm for the H2O2-forming enzyme and 271, 375 and 447 nm for the H2O-forming enzyme. Antibodies raised against the H2O2-forming enzyme or the H2O-forming enzyme reacted with their corresponding antigen, but did not cross-react. The amino-terminal regions of the two enzymes had completely different amino acid sequences.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2343-51"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-10-2343","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19242817","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 118

Formation of linear plasmid multimers promoted by the phage lambda Red-system in lon mutants of Escherichia coli. 大肠杆菌lon突变体中噬菌体λ - red系统促进线性质粒多聚体的形成。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2387

E Mythili, K Muniyappa

{"title":"Formation of linear plasmid multimers promoted by the phage lambda Red-system in lon mutants of Escherichia coli.","authors":"E Mythili, K Muniyappa","doi":"10.1099/00221287-139-10-2387","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2387","url":null,"abstract":"We report here the formation of plasmid linear multimers promoted by the Red-system of phage lambda using a multicopy plasmid comprised of lambda red alpha and red beta genes, under the control of the lambda cI857 repressor. Our observations have revealed that the multimerization of plasmid DNA is dependent on the red beta and recA genes, suggesting a concerted role for these functions in the formation of plasmid multimers. The formation of multimers occurred in a recBCD+ sbcB+ xthA+ lon genetic background at a higher frequency than in the isogenic lon+ host cells. The multimers comprised tandem repeats of monomer plasmid DNA. Treatment of purified plasmid DNA with exonuclease III revealed the presence of free double-chain ends in the molecules. Determination of the size of multimeric DNA, by pulse field gel electrophoresis, revealed that the bulk of the DNA was in the range 50-240 kb, representing approximately 5-24 unit lengths of monomeric plasmid DNA. We provide a conceptual framework for Red-system-promoted formation and enhanced accumulation of plasmid linear multimers in lon mutants of E. coli.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2387-97"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-10-2387","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19242821","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 9

Regulation of secreted protein production by filamentous fungi: recent developments and perspectives. 丝状真菌分泌蛋白产生的调控:最新进展和前景。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2295

D A MacKenzie, D J Jeenes, N J Belshaw, D B Archer

{"title":"Regulation of secreted protein production by filamentous fungi: recent developments and perspectives.","authors":"D A MacKenzie, D J Jeenes, N J Belshaw, D B Archer","doi":"10.1099/00221287-139-10-2295","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2295","url":null,"abstract":"Filamentous fungi, typically, are saprophytic organisms which, unlike yeasts, secrete a wide array of enzymes involved in the breakdown and recycling of complex polymers from both plant and animal tissues. This makes them attractive hosts for the production of secreted heterologous proteins (Jeenes et al., 1991; van den Hondel et al., 1991). In only a few examples, however, have the secreted yields of heterologous protein reached the gram per litre levels of many homologous fungal enzymes. In many cases, the problem does not appear to be at the level of transcription but, rather, occurs within the secretory pathway. Although the secretory process has barely been explored in filamentous fungi, we have attempted to identify areas upon which attention should be focused based on current knowledge gained from other systems. We also discuss recent developments in the dissection of transcriptional control in these organisms with particular reference to the interaction of regulatory proteins with fungal promoter regions and to the need for targeting expression cassettes to specific locations in the fungal genome. Understanding the detailed mechanisms of transcriptional control will help in designing modified promoter elements or regulatory factors optimized for a given set of growth conditions. Coupled with the proposed study of the secretory pathway, this should improve the yields of secreted heterologous proteins produced by filamentous fungi.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2295-307"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19242813","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 75

Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases. 钙酸不动杆菌BD413脂溶系统生长相依赖性表达:一个酯酶编码基因的克隆。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2329

R G Kok, V M Christoffels, B Vosman, K J Hellingwerf

{"title":"Growth-phase-dependent expression of the lipolytic system of Acinetobacter calcoaceticus BD413: cloning of a gene encoding one of the esterases.","authors":"R G Kok, V M Christoffels, B Vosman, K J Hellingwerf","doi":"10.1099/00221287-139-10-2329","DOIUrl":"https://doi.org/10.1099/00221287-139-10-2329","url":null,"abstract":"Acinetobacter calcoaceticus BD413, when grown in batch culture in nutrient broth, produces both extracellular lipase activity and cell-bound esterase activity during and after the transition between exponential growth and the stationary phase. From a library of A. calcoaceticus DNA in Escherichia coli, plasmids were isolated that enabled E. coli to grow on media with tributyrin as the sole carbon source. Assays with model substrates classified the product of the cloned gene as an esterase. Via deletion analysis, the esterase gene was mapped on a 1.8 kbp chromosomal DNA fragment. This fragment was sequenced and found to contain one open reading frame, termed estA, which encodes a protein of 40.0 kDa. The amino acid sequence of this protein shows homology to a number of lipolytic enzymes, most notably to esterases. Deletion of estA only partially abolished cell-bound esterase activity in A. calcoaceticus, indicating that BD413 forms at least two esterases. Both esterases show the same temporal regulation of expression. beta-Galactosidase activity was measured in strains in which a promoterless lacZ gene was inserted into estA. Induction of lacZ expression in these strains also occurred at the end of exponential growth in batch cultures, indicating that production of the esterase is regulated at the genetic level.","PeriodicalId":15884,"journal":{"name":"Journal of general microbiology","volume":"139 10","pages":"2329-42"},"PeriodicalIF":0.0,"publicationDate":"1993-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1099/00221287-139-10-2329","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19242816","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 93

New derivatives of TOL plasmid pWW0. TOL质粒pWW0的新衍生物。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2379

I Sarand, A Mäe, R Vilu, A Heinaru

引用次数: 2

Use of a triplex polymerase chain reaction for the detection and differentiation of Mycoplasma pneumoniae and Mycoplasma genitalium in the presence of human DNA. 在人类DNA存在的情况下，使用三重聚合酶链反应检测和分化肺炎支原体和生殖支原体。

Journal of general microbiology Pub Date : 1993-10-01 DOI: 10.1099/00221287-139-10-2431

N Cadieux, P Lebel, R Brousseau

引用次数: 67