Library

X
feed icon rss

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
  • 1
    Electronic Resource
    Electronic Resource
    Role of the transcriptional activator RocR in the arginine-degradation pathway of Bacillus subtilis (1997)
    Oxford UK : Blackwell Science Ltd
    Molecular microbiology 24 (1997), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: In Bacillus subtilis, genes involved in arginine and ornithine catabolism constitute two operons, rocABC and rocDEF. Inducible expression of these two operons is SigL-dependent and requires the transcriptional activator RocR. RocR is a member of the NtrC/NifA family of regulators. To study the molecular mechanisms leading to the activation of RocR, we constructed a series of mutants affected in various steps of arginine catabolism. Results obtained using these mutants strongly suggest that the true inducer is ornithine or citrulline. Constitutive mutants of rocR containing either missense mutations, frameshift mutations resulting from deletions, or in-frame deletions leading to the synthesis of N-terminal truncated RocR polypeptides were obtained. Analysis of these mutants indicates that the N-terminal part of RocR is an intramolecular repressor domain. AhrC is a second positive regulatory protein of the rocABC and rocDEF operons. Two missense mutations modifying the N-terminal domain of RocR led to high constitutive expression of the Roc regulon in the absence of AhrC. Constitutive RocR proteins still require the presence of UAS1 and therefore probably bending of the DNA region located between the UAS1 and the promoter, suggesting that AhrC is not involved in DNA bending which facilitates interaction between RocR and σ54-RNA polymerase. We suggest that the positive role of AhrC involves protein–protein interaction with RocR.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1997.3881754.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    A role for mRNA secondary structure in the control of translation initiation (1982)
    [s.l.] : Nature Publishing Group
    Nature 295 (1982), S. 616-618 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The 701-708 double mutant was constructed in vivo by homologous recombination within the 26 base pairs (bp) that separate the two mutations. The strategy used in this construction, described in Fig. 3 legend, involved three steps. First, a A transducing phage carrying the lamB-lacZ hybrid gene 52-4 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/295616a0
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Identification of a new locus, sacV, involved in the regulation of levansucrase synthesis in Bacillus subtilis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 44 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: An EcoRI DNA fragment of 0.5 kb specifically stimulating levansucrase synthesis was cloned in Bacillus subtilis. Transcriptional stimulation of levansucrase expression was observed after induction by sucrose when the sequence was present on a multicopy plasmid in B. subtilis. The nucleotide sequence of the DNA fragment was determined. The involvement of a putative peptide is discussed. This fragment located on the chromosomal map of B. subtilis near the dal locus defines a new locus, sacV, of the sucrose metabolic system.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02238.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 4
    Electronic Resource
    Electronic Resource
    Cloning of the sacS gene encoding a positive regulator of the sucrose regulon in Bacillus subtilis (1987)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 41 (1987), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The sacS gene controls the expression of 2 saccharolytic enzymes in Bacillus subtilis (sucrase and levansucrase).This paper describes a recombinant plasmid containing a mutant allele, sacSc. The plasmid was isolated from a B. subtilis DNA bank established in Escherichia coli. Moreover, it was shown that the sacSc allele, placed on a high-copy plasmid, is dominant over the wild-type chromosomal sacS+ allele. This result strongly suggests that the sacS gene encodes a positive regulatory protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1987.tb02184.x
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 5
    Electronic Resource
    Electronic Resource
    A DNA sequence containing the control sites for gene malT and for the malPQ operon (1982)
    Springer
    Molecular genetics and genomics 185 (1982), S. 88-92 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The order of 802 base pairs was established in a DNA segment containing the promoter for malPQ which is one of the three maltose operons, and the promoter for malT, the positive regulator gene of the maltose regulon. The determination of the amino-terminal sequence of the MalT protein allowed us to identify the beginning of the malT gene on the sequence. The position of the malP gene was deduced from the published amino-terminal sequence of maltodextrin phosphorylase. A total of 611 base pairs separate the initiation codons for these two genes, which are transcribed in opposite directions. This large intergenic region does not code for any polypeptide of significant size. The main features of this sequence are discussed in terms of the regulation known to operate on malT and malPQ expression.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333795
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 6
    Electronic Resource
    Electronic Resource
    Characterization of the levanase gene of Bacillus subtilis which shows homology to yeast invertase (1987)
    Springer
    Molecular genetics and genomics 208 (1987), S. 177-184 
    Details
    ISSN: 1617-4623
    Keywords: Bacillus subtilis ; Levanase ; Nucleotide sequence ; Yeast invertase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The structural gene for the enzyme levanase of Bacillus subtilis (SacC) was cloned in Escherichia coli. The cloned gene was mapped by PBS1 transduction near the sacL locus on the B. subtilis chromosome, between leu4 and aroD. Expression of the enzyme was demonstrated both in B. subtilis and in E. coli. The presence of sacC allowed E. coli to grow on sucrose as the sole carbon source. The complete nucleotide sequence of sacC was determined. It includes an open reading frame of 2,031 bp, coding for a protein with calculated molecular weight of 75,866 Da, including a putative signal peptide similar to precursors of secreted proteins found in Bacilli. The apparent molecular weight of purified levanase is 73 kDa. The sacC gene product was characterized in an in vitro system and in a minicellproducing strain of E. coli, confirming the existence of a precursor form of levanase of about 75 kDa. Comparison of the predicted aminoacid sequence of levanase with those of the two other known β-D-fructofuranosidases of B. subtilis indicated a homology with sucrase, but not with levansucrase. A stronger homology was detected with the N-terminal region of yeast invertase, suggesting the existence of a common ancestor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330439
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
  • 7
    Electronic Resource
    Electronic Resource
    Mutants which make more malT product, the activator of the maltose regulon in Escherichia coli (1980)
    Springer
    Molecular genetics and genomics 178 (1980), S. 589-595 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Some of the previously described malT-lacZ fusion strains (Débarbouillé and Schwartz, 1979) produce very low amounts of β-galactosidase activity and hence grow poorly on lactose. Spontaneous mutants growing faster on lactose have been isolated. Some of the mutations map in, or close to, the promoter of the hybrid gene. They lead to an increased production of the hybrid proteins, which then become detectable on polyacrylamide gels. This effect is cis dominant. When the mutations, called malT q+, are transduced into a malT ++ background the resulting transductants express the three maltose operons in a partially constitutive way. The malT q+ mutations therefore represent a new type of constitutive mutation. Their existence provides further evidence for the previously proposed model of positive regulation in the maltose regulon. In addition they should facilitate the purification of the malT product, and the indentification of the malT promoter on the DNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337865
    Library Location Call Number Volume/Issue/Year Availability
    BibTip Others were also interested in ...
    Paper (German National Licenses)
    Fulltext
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...