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  • 1
    Electronic Resource
    Electronic Resource
    Building a science in Japan: The formative decades of Molecular Biology (1993)
    Springer
    Journal of the history of biology 26 (1993), S. 499-517 
    Details
    ISSN: 1573-0387
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , History
    Notes: Abstract I am honored to have been invited to participate in this Workshop on Comparative Studies of Building Molecular Biology, with a discussion of Japanese experiences in constructing a science — in this case, the discipline of molecular biology. As I understand it, the construction of a science must be equivalent to building a new culture. My having given this title to my paper suggests that I have enough knowledge about the subject to perhaps even extrapolate its course into the future — which I do not. What I do have is a sincere admiration of my old friends and colleagues, in Japan and elsewhere, who together tried to build a new science of molecular biology in Japan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01062059
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  • 2
    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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  • 3
    Electronic Resource
    Electronic Resource
    Isolation of conditionally lethal amber mutations affecting synthesis of the nusA protein of Escherichia coli (1983)
    Springer
    Molecular genetics and genomics 190 (1983), S. 196-203 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Amber mutants (am3 and am4) of Escherichia coli K12 defective in the synthesis of nusA protein (Friedman 1971) were isolated from a strain harboring an amber suppressor (sup-126) that is active only at low temperatures. These mutants grew at low temperature (30°C) but did not grow at temperatures above 38°C. Complementation experiments with plasmids carrying the nusA +gene and its derivatives or with plasmids carrying the nusA1 or am4 mutation indicated that the mutations am3, am4 and nusA1 affected the same gene function. Analysis of proteins produced by minicells containing a plasmid demonstrated that the plasmid pYN87, which can complement the nusA1 and amber mutations, codes for three bacterial proteins, a truncated nusA gene product (61 K), argG gene product (48 K) and a 21 K dalton protein, and that the am4 mutation affects the synthesis of only NusA protein. λNam7 (and λNam7Nam53) phages could grow on these amber mutants at 32°C but not on the parental strain. Spontaneous temperature-resistant revertants of the amber mutants simultaneously lost the ability to permit λNam7 phage development, indicating that the two phenotypes are due to a single mutation. These results suggest that the nusA gene function is essential for the growth of E. coli, and that the λN function is dispensable for phage development if the nusA gene is defective.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330640
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  • 4
    Electronic Resource
    Electronic Resource
    Organization and expression of the dnaJ and dnaK genes of Escherichia coli K12 (1978)
    Springer
    Molecular genetics and genomics 164 (1978), S. 1-8 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A temperature-sensitive mutation in the dnaJ gene of Escherichia coli K12 is described which affects replication of the bacterial DNA. The gene is located adjacent to the dnaK gene described previously (Saito and Uchida, 1977). The physical and functional organization of the dnaJ-dnaK region was studied in detail by analyzing the heteroduplexes and functions of various deletion mutants of λdnaJdnaK, a transducing phage carrying both of the dna genes. The sizes of dnaJ and dnaK cistrons were estimated to be at most 1.2±0.5 and 2.1±0.4 kilobases, respectively. In vivo expression of the dnaJ function by various deletion phages indicated that the dnaK and dnaJ cistrons were transcribed from a promoter located at the head of the dnaK cistron, dnaJ being downstream to dnaK. Presence of a weak promoter which reads only the dnaJ cistron was also suggested. A simple method for isolating independent deletion mutants of phage λ was described.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267592
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  • 5
    Electronic Resource
    Electronic Resource
    A transducing λ phage carrying grpE, a bacterial gene necessary for λ DNA replication, and two ribosomal protein genes, rpsP (S16) and rplS (L19) (1978)
    Springer
    Molecular genetics and genomics 165 (1978), S. 247-256 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A grpE mutation of Escherichia coli K12, which blocks DNA replication of the phage λ (Saito and Uchida, 1977), was mapped at 56 min on the standard genetic map. A transducing λ phage, λgrpE22, carrying the wild type allele of the grpE gene was constructed in vitro. Structures of λgrpE22 and its viable deletion derivatives were determined by electron microscopic analyses of appropriate heteroduplexes. Proteins coded by the bacterial DNA incorporated into the transducing phages were detected by two-dimensional gel electrophoresis. The results showed that the product of the grpE gene is a weakly acidic protein of molecular weight 24,000. Structural genes for two ribosomal proteins, rplS (L19) and rpsP (S16) were also shown to be carried by λgrpE22.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332523
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  • 6
    Electronic Resource
    Electronic Resource
    Suppressors of temperature-sensitive mutations in a ribosomal protein gene, rpsL (S12), of Escherichia coli K12 (1985)
    Springer
    Molecular genetics and genomics 199 (1985), S. 381-387 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Temperature-sensitive (ts) mutations were isolated within a ribosomal protein gene (rpsL) of Escherichia coli K12. Mutations were mapped by complementation using various transducing phages and plasmids carrying the rpsL gene, having either a normal or a defective promoter for the rpsL operon. One of these mutations, ts118, resulted in a mutant S12 protein which behaved differently from the wild-type S12 on CM-cellulose column chromatography. Suppressors of these ts mutations were isolated and characterized; one was found to be a mutation of a nonribosomal protein gene which was closely linked to the RNAase III gene on the E. coli chromosome. This suppressor, which was recessive to its wild-type allele, was cloned into a transducing phage and mapped finely. A series of cold-sensitive mutations, affecting the assembly of ribosomes at 20°C, was isolated within the purL to nadB region of the E. coli chromosome and one group, named rbaA, mapped at the same locus as the suppressor mutation, showing close linkage to the RNAase III gene.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330746
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  • 7
    Electronic Resource
    Electronic Resource
    DNA sequencing of the Escherichia coli ribonuclease III gene and its mutations (1985)
    Springer
    Molecular genetics and genomics 201 (1985), S. 25-29 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A 0.7 kb DNA fragment of the Escherichia coli K12 chromosome was shown to contain the structural gene for RNAse III (rnc). The DNA sequence of the gene was determined and its alteration in an RNAse III defective mutant, AB301-105, was identified. DNA sequence analysis also showed that a secondary-site suppressor of a temperature-sensitive mutation in the E. coli ribosomal protein gene, rpsL, occurred within the rnc gene, providing genetic evidence for the interaction of ribosomal proteins with RNAse III, which in turn acts on the nascent ribosomal RNA during assembly of ribosomes in E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397981
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  • 8
    Electronic Resource
    Electronic Resource
    Isolation and characterization of herC, a mutation of Escherichia coli affecting maintenance of ColE1 (1989)
    Springer
    Molecular genetics and genomics 219 (1989), S. 333-340 
    Details
    ISSN: 1617-4623
    Keywords: ColE1 replication ; Primer RNA ; Suppressor mutation ; RF2 ; Ribonuclease H
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two modes of ColE1 DNA replication are known, one dependent on RNase H, and the other RNase H independent. The cer114 mutant of the ColE1 replicon is defective in both modes and carries a single base pair alteration 95 by upstream of the replication origin. An Escherichia coli mutant which restored maintenance of the cer114 replicon was isolated. This host suppressor mutant is defective in RNase H and carries a herC, mutation located at 62 min of the E. coli chromosome. The herC, mutation is recessive to its wild-type allele and supports maintenance of the mutant replicon in the absence of RNase H. The herC, mutation alone conferred cold-sensitive growth, suggesting that the herC, gene product is essential for cell growth. The 1832 by E. coli DNA fragment, containing the wild-type allele of the herC, mutation, was cloned and an open reading frame for the HerC protein was determined.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00259604
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