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  • 1
    Electronic Resource
    Electronic Resource
    Purification and sequencing of the active site tryptic peptide from penicillin-binding protein 1b of Escherichia coli (1985)
    s.l. : American Chemical Society
    Biochemistry 24 (1985), S. 3448-3453 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00335a009
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  • 2
    Electronic Resource
    Electronic Resource
    Acriflavine as an Effective Agent for eliminating F -factor in Escherichia coli K -12 (1957)
    [s.l.] : Nature Publishing Group
    Nature 180 (1957), S. 655-656 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] An overnight culture of F -f cells is inoculated into a nutrient broth containing 'Kyokuto' broth 10 gm., 'Kyokuto' peptone 10 gm., sodium chloride 2 gm., and distilled water 1 litre or 'Difco' broth 10 gm., 'Difeo' peptone 10 gm., and distilled water 1 litre, with a sublethal concentration of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/180655a0
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  • 3
    Electronic Resource
    Electronic Resource
    Effects of radioactive decay on the autonomous replicatin of anEscherichia coli episome (1964)
    Springer
    Molecular genetics and genomics 95 (1964), S. 184-194 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary TheE. coli episomeF 13 loses its capacity for autonomous replication when the integrity of the molecule is impaired by the decay of32P atoms incorporated into its polynucleotide chains. Upon further division of the host bacteria, the distal fragments near the episomal terminus are eliminated, whereas, the proximal fragments near the episomal origin may survive as heterogenotes attached to the host chromosome.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00894919
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  • 4
    Electronic Resource
    Electronic Resource
    Further temperature-sensitive mutants ofEscherichia coli with altered ribosomal proteins (1977)
    Springer
    Molecular genetics and genomics 152 (1977), S. 239-243 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Various alterations in ribosomal proteins were detected in forty-one mutants ofE. coli isolated as temperature-sensitive mutants. Out of these, six are new classes of mutants harboring mutations in proteins S3, L5, L7 (L12), L29, L30 and L33. One of them apparently lacks protein L7 of the large subunit. These mutants together with those reported previously (Isono et al., 1976) total one hundred and one ribosomal mutants in thirty different proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00693076
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  • 5
    Electronic Resource
    Electronic Resource
    Isolation and characterization of temperature-sensitive mutants of Escherichia coli with altered ribosomal proteins (1976)
    Springer
    Molecular genetics and genomics 149 (1976), S. 297-302 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ribosomal proteins of temperature-sensitive mutants of Escherichia coli isolated independently after mutagenesis with nitrosoguanidine were analyzed by two-dimensional gel electrophoresis. Out of 400 mutants analyzed, 60 mutants (15%) showed alterations in a total of 22 different ribosomal proteins. The proteins altered in these mutants are S2, S4, S6, S7, S8, S10, S15, S16, S18, L1, L3, L6, L10, L11, L14, L15, L17, L18, L19, L22, L23 and L24. A large number of them (25 mutants) have mutations in protein S4 of the small subunit, while four mutants showed alterations in protein L6 of the large subunit. The importance of these mutants for structural and functional analyses of ribosomes is discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00268531
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  • 6
    Electronic Resource
    Electronic Resource
    Suppressor genes of a dnaA temperature sensitive mutation in Escherichia coli (1982)
    Springer
    Molecular genetics and genomics 187 (1982), S. 67-71 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Recombinant plasmids were constructed from EcoRI digests of Escherichia coli chromosomal DNA and pMB9 DNA by selecting for suppression of a dnaA−T46 temperature-sensitive mutation. Two types of plasmid capable of suppressing the dnaA mutation were isolated. They did not carry any genetic markers around dnaA and physical mapping with various restriction enzymes showed that neither of the plasmids contained the dnaA gene. One plasmid, pYT47, was characterized further and the protein responsible for the suppression was identified by two-dimensional gel electrophoresis. The molecular weight of the suppressor protein was about 68 Kdal and thus is clearly different from the dnaA gene product.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00384385
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  • 7
    Electronic Resource
    Electronic Resource
    Gene affecting longevity of messenger RNA: A mutant ofEscherichia coli with altered mRNA stability (1977)
    Springer
    Molecular genetics and genomics 154 (1977), S. 279-285 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary we have screened 897 temperature sensitive growth mutants ofE. coli for mutant strains showing longer mRNA half-life. The fate of pulse-labelled RNA was examined at 42° C after cessation of RNA synthesis and with prior exposure to nonpermissive temperature (42° C). Eight stains showed altered turn-over of RNA (presumably mRNA), and further analysis on mutant strain JE15144 indicated that the stability of pulse-labeled RNA as well as of tryptophan (trp) mRNA increased four to seven fold over its parental strain at 42° C. At 4 min or 10 min after addition of rifampicin, some 70 to 80% of polyribosome in the growing cells could still be conserved in JE15144 cultured at the nonpermissive temperature while little, if any, polyribosomes remained in its parental strain (PA3092) under the same condition. Two generation times were required for complete stoppage of growth of this mutant strain after shifting to 42° C, and protein synthesis continued at a significant, but slightly reduced, rate at 42° C. However, functional decay of mRNA in the mutant strain, with respect to the capacity for producing peptides, appeared to be similar to the parent strain, with half-lives of 3.5 min in PA3092 and 4.7 min in JE15144.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00571283
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  • 8
    Electronic Resource
    Electronic Resource
    Murein-lipoprotein of Escherichia coli: A protein involved in the stabilization of bacterial cell envelope (1978)
    Springer
    Molecular genetics and genomics 167 (1978), S. 1-9 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two independent mutants of Escherichia coli lacking murein-lipoprotein have been found. One mutant whose mutation was named lpo was subjected to detailed analyses. The absence of both found and unbound lipoproteins was shown by electrophoretic analysis of 14C-arginine labelled membrane proteins of the mutant. Nor was serologically cross-reacting material detected in the mutant by the Ouchterlony-method. Sequestering magnesium from mutant cell suspensions by ethylenediaminetetraacetic acid caused cell lysis, which was prevented in the presence of 0.5 M sucrose. Incubation in culture media at a very low level of magnesium resulted in the formation of blebs in the mutant. Examination of mutant cells by electron microscopy showed that the outer membrane of the mutant was uneven with small irregular protuberances, some of which pinched off forming vesicles of various sizes. Phosphotungstate used for negative-staining penetrated into the periplasmic space of the mutant cells. The mutants leaked a considerable fraction of their periplasmic enzymes. These physiological and morphological alterations in the lipoproteinless mutant suggest that murein-lipoprotein helps to maintain the outer envelope structure by connecting the outer membrane with murein so that the outer membrane may fulfil its physiological functions as a barrier to the environment.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00270315
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  • 9
    Electronic Resource
    Electronic Resource
    Replication origin of the Escherichia coli K-12 chromosome: The size and structure of the minimum DNA segment carrying the information for autonomous replication (1980)
    Springer
    Molecular genetics and genomics 178 (1980), S. 9-20 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A DNA fragment containing the replication origin of the Escherichia coli K-12 chromosome was inserted in two orientations at either the BamHI or SalI site of pBR322 DNA. All the resulting hybrid plasmids were found to replicate in both polA and polA + cells, whereas pBR322 replicates only in polA + cells. This characteristic provided a method for assaying the autonomously replicating ability (Ori function) of the E. coli origin. In order to define the minimum DNA region (ori) that determines Ori function, deletions of various sizes were introduced from either side of the ori-containing segment in the hybrid plasmids by in vitro techniques, and the correlation between the Ori phenotype and nucleotide sequence of the deletion derivatives was analyzed. It was found that the left end of ori is between positions 23 and 35, and the right end is either position 266 or 267 in our nucleotide coordinate (Sugimoto et al., 1979). Therefore, ori is present within a region of minimum 232 base pairs and maximum 245 base pairs in length. The Ori+ and Ori- phenotypes were clearly resolved at both sides of these boundaries by the above assay procedure. To obtain information about the effect of mutations in the internal region of the defined ori stretch, short sequences were inserted or deleted in vitro in the vicinity of several restriction sites within ori on the hybrid plasmids. Most of these plasmids carrying modified sequences showed Ori- phenotype, suggesting that most parts of the ori stretch play important roles in Ori function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267207
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  • 10
    Electronic Resource
    Electronic Resource
    Mutants of Escherichia coli defective in penicillin-insensitive murein DD-endopeptidase (1983)
    Springer
    Molecular genetics and genomics 189 (1983), S. 215-221 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two mutants of Escherichia coli that are deficient in the penicillin-insensitive DD-endopeptidase have been isolated. The strain JE10874 (mepA) has about 10%–20% of the residual activity and another strain, JE10368 (mepB) has 40%–50% of the activity found in the wild-type, parental strain, PA3092. The penicillin-insensitive endopeptidase is a periplasmic enzyme. Genetic mapping studies show that the mutation mepA is located close to aroC (50 min) and the other mutation, mepB, is very close to malE (91 min) on the chromosome. These mutants grow normally under a wide range of growth conditions; other phenotypic properties of the mutants are very similar to those of the parent strain. A double mutant (mepA mepB), and a triple mutant (mepA mepB dacB), deficient in both penicillin-insensitive and penicillin-sensitive endopeptidases, were constructed. Again, these mutants grew normally. We conclude that either the very low level of residual enzyme activity in the mutants is enough for their survival or that the penicillin-insensitive endopeptidase is not essential for survival under laboratory conditions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337807
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