SSG1, a gene encoding a sporulation-specific 1,3-beta-glucanase in Saccharomyces cerevisiae.San Segundo, P; Correa, J; Vazquez de Aldana, C R; del Rey, F
doi: N/Apmid: 8509335
SSG1, a gene encoding a sporulation-specific 1,3-beta-glucanase in Saccharomyces cerevisiae. P San Segundo , J Correa , C R Vazquez de Aldana and F del Rey Instituto de Microbiología-Bioquímica, Facultad de Biología, Universidad de Salamanca, Consejo Superior de Investigaciones Cientificas, Spain. ABSTRACT In Saccharomyces cerevisiae, the meiotic process is accompanied by a large increase in 1,3-beta-glucan-degradative activity. The molecular cloning of the gene (SSG1) encoding a sporulation-specific exo-1,3-beta-glucanase was achieved by screening a genomic library with a DNA probe obtained by polymerase chain reaction amplification using synthetic oligonucleotides designed according to the nucleotide sequence predicted from the amino-terminal region of the purified protein. DNA sequencing indicates that the SSG1 gene specifies a 445-amino-acid polypeptide (calculated molecular mass, 51.8 kDa) showing extensive similarity to the extracellular exo-1,3-beta-glucanases encoded by the EXG1 gene (C. R. Vazquez de Aldana, J. Correa, P. San Segundo, A. Bueno, A. R. Nebreda, E. Mendez, and F. del Rey, Gene 97:173-182, 1991). The N-terminal domain of the putative precursor is a very hydrophobic segment with structural features resembling those of signal peptides of secreted proteins. Northern (RNA) analysis reveals a unique SSG1-specific transcript, 1.7 kb long, which can be detected only in sporulating diploids (MATa/MAT alpha) but does not appear in vegetatively growing cells or in nonsporulating diploids (MAT alpha/MAT alpha) when incubated under nitrogen starvation conditions. The meiotic time course of SSG1 induction indicates that the gene is transcribed only in the late stages of the process, beginning at the time of meiosis I and reaching a maximum during spore formation. Homozygous ssg1/ssg1 mutant diploids are able to complete sporulation, although with a significant delay in the appearance of mature asci. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3823-3837 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by San Segundo, P. Articles by del Rey, F. Search for related content PubMed PubMed citation Articles by San Segundo, P. Articles by del Rey, F. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
DNA sequence and mutational analysis of genes involved in the production and resistance of the antibiotic peptide trifolitoxin.Breil, B T; Ludden, P W; Triplett, E W
doi: N/Apmid: 8509324
The 7.1-kb fragment of Rhizobium leguminosarum bv. trifolii T24 DNA which confers trifolitoxin production and resistance to nonproducing, sensitive Rhizobium strains (E. W. Triplett, M. J. Schink, and K. L. Noeldner, Mol. Plant-Microbe Interact. 2:202-208, 1989) was subcloned, sequenced, and mutagenized with a transcriptional fusion cassette. The sequence of this fragment revealed seven complete open reading frames, tfxABCDEFG, all transcribed in the same direction. TfxA has an 11-amino-acid carboxy terminus identical to the known amino acid sequence of the trifolitoxin backbone, DIGGSRXGCVA, where X is an UV-absorbing chromophore. This is evidence that trifolitoxin is synthesized ribosomally as a prepeptide that is posttranslationally modified to yield the active peptide. TfxB shows 27.6% identity with McbC, a protein required for the production of the ribosomally synthesized antibiotic microcin B17. Tn3GUS transcriptional fusion insertions in tfxA, tfxB, tfxD, or tfxF caused a nonproducing, trifolitoxin-resistant phenotype and confirmed the direction of transcription of these frames. No insertion mutations were found in tfxE or tfxG. Sequence analysis along with insertion and deletion mutation analysis suggest that (i) trifolitoxin is synthesized ribosomally from tfxA; (ii) tfxA, tfxE, and tfxG have their own promoters; (iii) TfxG is required for immunity; (iv) TfxB, TfxD, and TfxF are required for trifolitoxin production; and (v) the UV-absorbing chromophore is derived from glutamine. J Bacteriol. 1993 June; 175(12): 3693-3702
Cloning and sequencing of a gene encoding carminomycin 4-O-methyltransferase from Streptomyces peucetius and its expression in Escherichia coli.Madduri, K; Torti, F; Colombo, A L; Hutchinson, C R
doi: N/Apmid: 8509343
Cloning and sequencing of a gene encoding carminomycin 4-O-methyltransferase from Streptomyces peucetius and its expression in Escherichia coli. K Madduri , F Torti , A L Colombo and C R Hutchinson School of Pharmacy, University of Wisconsin-Madison 53706. ABSTRACT Sequence analysis of a portion of the Streptomyces peucetius daunorubicin biosynthetic gene cluster revealed a complete open reading frame (dnrK) that showed DNA and protein sequence homology to several O-methyltransferases. Expression of dnrK in Streptomyces lividans and Escherichia coli was done to show that this gene codes for carminomycin 4-O-methyltransferase. The deduced carminomycin 4-O-methyltransferase protein shows a conserved nucleotide binding site for its S-adenosyl-L-methionine cofactor. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3900-3904 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Madduri, K. Articles by Hutchinson, C. R. Search for related content PubMed PubMed citation Articles by Madduri, K. Articles by Hutchinson, C. R. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Vibrio parahaemolyticus has a homolog of the Vibrio cholerae toxRS operon that mediates environmentally induced regulation of the thermostable direct hemolysin gene.Lin, Z; Kumagai, K; Baba, K; Mekalanos, J J; Nishibuchi, M
doi: N/Apmid: 8509337
In an effort to identify the regulatory gene controlling the expression of the tdh gene, encoding the thermostable direct hemolysin of Vibrio parahaemolyticus, we examined total DNA of AQ3815 (a Kanagawa phenomenon-positive strain) for sequences homologous to that of the toxR gene of Vibrio cholerae. The extracted DNA gave a weak hybridization signal under reduced-stringency conditions with a toxR-specific DNA probe. Cloning and sequence analysis of the probe-positive sequence revealed an operon (Vp-toxRS) which was highly similar to the toxRS operon of V. cholerae (Vc-toxRS) (52 and 62% similarities in the two genes, respectively). The deduced amino acid sequences of the Vp-toxRS gene products (Vp-ToxRS) contained regions similar to the proposed transmembrane and activity domains of the Vc-toxRS gene products (Vc-ToxRS). All clinical and environmental strains of V. parahaemolyticus examined possessed the Vp-toxRS genes. In the presence of Vp-ToxS, Vp-ToxR promoted expression of the tdh2 gene, one of two tdh genes (tdh1 and tdh2) carried by Kanagawa phenomenon-positive strains. The DNA sequence located 144 bp upstream of the tdh2 coding region was shown to be important for the Vp-ToxR-stimulated expression of the tdh2 gene in an Escherichia coli background. Comparative analysis of AQ3815 and its isogenic Vp-toxR null mutant gave the following results: (i) Vp-ToxR promoted, in an AQ3815 background, expression of the tdh gene to different degrees in various culture media, with KP broth (2% peptone, 0.5% NaCl, 0.03 M KH2PO4, pH 6.2) being most effective (12-fold); (ii) the promotion of tdh gene expression in KP broth was at the level of transcription; and (iii) Vp-ToxR was essential for demonstration of enterotoxic activity of AQ3815 in the rabbit ileal loop, a model previously used to demonstrate thermostable direct hemolysin-mediated enterotoxic activity of AQ3815. These results demonstrate that Vp-ToxR and Vc-ToxR share a strikingly similar function, i.e., direct stimulation at the transcriptional level of the gene encoding a major virulence determinant (enterotoxin) of a Vibrio species. J Bacteriol. 1993 June; 175(12): 3844-3855
Identification, isolation, and characterization of the structural gene encoding the delta' subunit of Escherichia coli DNA polymerase III holoenzyme.Carter, J R; Franden, M A; Aebersold, R; McHenry, C S
doi: N/Apmid: 8509334
Identification, isolation, and characterization of the structural gene encoding the delta' subunit of Escherichia coli DNA polymerase III holoenzyme. J R Carter , M A Franden , R Aebersold and C S McHenry University of Colorado Health Sciences Center, Department of Biochemistry, Biophysics and Genetics, Denver, Colorado 80262. ABSTRACT The gene encoding the delta' subunit of DNA polymerase III holoenzyme, designated holB, was cloned by a strategy in which peptide sequence was used to derive a DNA hybridization probe. The gene maps to 24.95 centisomes of the chromosome. Sequencing of holB revealed a 1,002-bp open reading frame predicted to produce a 36,936-Da protein. The gene has a ribosome-binding site and promoter that are highly similar to the consensus sequences and is flanked by two potential open reading frames. Protein sequence analysis of delta' revealed a high degree of similarity to the dnaX gene products of Escherichia coli and Bacillus subtilis, including one stretch of 10 identical amino acid residues. A lesser degree of similarity to the gene 44 protein of bacteriophage T4 and the 40-kDa protein of the A1 complex (replication factor C) of HeLa cells was seen. The gene, when placed into a tac promoter-based expression plasmid, directed expression of two proteins of similar size. By immunodetection with anti-holoenzyme immunoglobulin G, both proteins are judged to be products of holB. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3812-3822 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Carter, J. R. Articles by McHenry, C. S. Search for related content PubMed PubMed citation Articles by Carter, J. R. Articles by McHenry, C. S. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases.Favre, D; Ngai, P K; Timmis, K N
doi: N/Apmid: 7685334
Relatedness of a periplasmic, broad-specificity RNase from Aeromonas hydrophila to RNase I of Escherichia coli and to a family of eukaryotic RNases. D Favre , P K Ngai and K N Timmis Département de Biochimie Médicale, Centre Médical Universitaire, Geneva, Switzerland. ABSTRACT The isolation, sequencing, and characterization of a periplasmic RNase gene from Aeromonas hydrophila AH1133 is described. Following subcloning of the gene on a 2.7-kb PstI fragment, its direction of transcription and approximate location were determined. Analysis of the nucleotide sequence reveals that the gene is 645 bp long, coding for 215 amino acid residues with a total molecular weight of 24,215. A typical leader sequence is present at the beginning of the corresponding protein. Computer analysis revealed strong local similarities to Escherichia coli RNase I and to the active site of a family of eukaryotic RNases. Expression studies indicate that the RNase natural promoter functions poorly in E. coli. In this organism, the enzyme is mainly localized in the cytoplasm and periplasm, although high levels of expression lead to significant release into the extracellular medium. Functional and physical characterizations further indicate that the periplasmic and cytoplasmic enzymes of A. hydrophila are likely to be the counterparts of E. coli RNase I and its cytoplasmic form RNase I*: as for the E. coli enzymes, the A. hydrophila RNase forms have similar sizes and show broad specificity, and the periplasmic form is more active towards natural polymer RNA than its cytoplasmic counterpart. Both forms are relatively thermosensitive and are reversibly inactivated by up to 0.6% sodium dodecyl sulfate. Southern hybridization revealed homology to E. coli K-12 and Shigella sp. genomic DNA, a finding which correlates with the presence of secreted RNases in these organisms. In contrast, species of phylogenetically closer genera, such as Vibrio and Plesiomonas, did not hybridize to the A. hydrophila RNase gene. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3710-3722 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Favre, D. Articles by Timmis, K. N. Search for related content PubMed PubMed citation Articles by Favre, D. Articles by Timmis, K. N. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa.Chow, C M; RajBhandary, U L
doi: N/Apmid: 8509325
Developmental regulation of the gene for formate dehydrogenase in Neurospora crassa. C M Chow and U L RajBhandary Department of Biology, Massachusetts Institute of Technology, Cambridge 02139. ABSTRACT We have isolated and characterized a gene, fdh, from Neurospora crassa which is developmentally regulated and which produces formate dehydrogenase activity when expressed in Escherichia coli. The gene is closely linked (less than 0.6 kb apart) to the leu-5 gene encoding mitochondrial leucyl-tRNA synthetase; the two genes are transcribed convergently from opposite strands. The expression patterns of these genes differ: fdh mRNA is found only during conidiation and early germination and is not detectable during mycelial growth, while leu-5 mRNA appears during germination and mycelial growth. The structure of the fdh gene was determined from the sequence of cDNA and genomic DNA clones and from mRNA mapping studies. The gene encodes a 375-amino-acid-long protein with sequence similarity to NAD-dependent dehydrogenases of the E. coli 3-phosphoglycerate dehydrogenase (serA gene product) subfamily. In particular, there is striking sequence similarity (52% identity) to formate dehydrogenase from Pseudomonas sp. strain 101. All of the residues thought to interact with NAD in the crystal structure of the Pseudomonas enzyme are conserved in the N. crassa enzyme. We have further shown that expression of the N. crassa gene in E. coli leads to the production of formate dehydrogenase activity, indicating that the N. crassa gene specifies a functional polypeptide. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3703-3709 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Chow, C. M. Articles by RajBhandary, U. L. Search for related content PubMed PubMed citation Articles by Chow, C. M. Articles by RajBhandary, U. L. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»
Growth rate paradox of Salmonella typhimurium within host macrophages.Abshire, K Z; Neidhardt, F C
doi: N/Apmid: 8509329
Growth rate paradox of Salmonella typhimurium within host macrophages. K Z Abshire and F C Neidhardt Department of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor 48109-0620. ABSTRACT The growth rate of Salmonella typhimurium U937 within host macrophages was estimated by two independent methods. The extent to which ribosomal protein L12 is acetylated to produce ribosomal protein L7 changes markedly with the growth rate. By this measure, the intracellular bacteria appeared to be growing rapidly. Measurements of viable bacteria, however, indicated that the bacteria were growing slowly. A solution of this apparent growth rate paradox was sought by treating U937 cells infected with S. typhimurium X3306 with ampicillin or chloramphenicol to help determine the number of bacteria that were actively growing and dividing in the intracellular condition. Use of these antibiotics showed that by 2 h after invasion, the intracellular bacteria consisted of at least two populations, one static and the other rapidly dividing. This finding implies that previously described changes in the gene expression of S. typhimurium are important for the survival and/or multiplication of the bacteria within the macrophage. CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? « Previous | Next Article » Table of Contents This Article J. Bacteriol. June 1993 vol. 175 no. 12 3744-3748 » Abstract PDF Classifications Research Article Services Email this article to a colleague Similar articles in ASM journals Alert me when this article is cited Alert me if a correction is posted Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of JB Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Load citing article information Citing articles via Web of Science Citing articles via Google Scholar Google Scholar Articles by Abshire, K. Z. Articles by Neidhardt, F. C. Search for related content PubMed PubMed citation Articles by Abshire, K. Z. Articles by Neidhardt, F. C. Related Content Load related web page information Social Bookmarking CiteULike Connotea Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter What's this? current issue December 2011, volume 193, issue 24 Alert me to new issues of JB About JB Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy JB RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • [email protected] Print ISSN: 0021-9193 Online ISSN: 1098-5530 Copyright © 2011 by the American Society for Microbiology. For an alternate route to JB .asm.org, visit: http://intl- JB .asm.org | More Info»