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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
    The role of cAMP in flagellation of Salmonella typhimurium (1975)
    Springer
    Molecular genetics and genomics 142 (1975), S. 289-298 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A mutational alteration either in adenylate cyclase (cya -) or in cyclic-3′5′-AMP (cAMP) receptor protein (crp -) rendered Salmonella typhimurium incapable of producing flagella. The amount of mRNA specific for flagellin in these mutants was almost negligible when assayed in an in vitro protein synthesizing system. A secondary mutation, cfs, partially suppressing the cya - mutation, was identified among the revertants of cya -. A mutation in the same cistron as cfs resulted in a non-flagellate phenotype either by itself or in combination with cfs. The cistron, which was given the gene symbol flaT, was located between flaE and flaL. It was suggested that cAMP receptor protein together with cAMP modulates the gene flaT, which in turn acts as a positive effector on the synthesis of active mRNA specific for flagellin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271253
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  • 3
    Electronic Resource
    Electronic Resource
    Overlapping of the coding regions for α and γ components of penicillin-binding protein 1 b in Escherichia coli (1984)
    Springer
    Molecular genetics and genomics 196 (1984), S. 449-457 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The mode of biosynthesis of penicillin-binding protein(PBP)-1 b in Escherichia coli was investigated by use of the plasmid carrying the ponB(PBP-1 b) gene region. Analyses of the products synthesized in minicells and in vitro showed that PBP-1 b was synthesized as two molecular species corresponding to the α and γ components of PBP-1 b. The coding regions for the α and γ components were located within the ca. 3.7 kb MluI-HincII fragment and transcribed in the direction from the HincII to the MluI site. The capacity for producing the α component was abolished by a deletion extending to the MluI site ca. 0.7 kb inward from the HincII end of the ca. 3.7 kb fragment; the remaining 3.0 kb region with the MluI site at both ends directed the production of the γ component alone. The production of the γ component was enough to correct all the known defects caused by a ponB mutation. In addition to these results, the analyses for cross-reacting materials produced in correspondence to the various deletions indicated that the coding regions for the α and γ components overlapped and that the N-terminal portion was responsible for the difference between the two components. The distal region about 0.7 kb long inward from the MluI end of the MluI-HincII fragment was dispensable for producing the functional PBP-1 b, although the PBP-1 b produced was curtailed. By a larger distal deletion reaching almost to the middle of the MluI-HincII fragment, the polypeptide produced for PBP-1 b lost the ability to bind penicillin and still retained a low but significant activity for glycan synthesis. We suggest, therefore, that the polypeptide portion required for transglycosylase activity resides on the N-terminal half of PBP-1 b, followed by the middle portion necessary for penicillin-binding and the C-terminal part dispensable for the function of PBP-1 b.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00436192
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  • 4
    Electronic Resource
    Electronic Resource
    Escherichia coli parA is an allele of the gyrB gene (1989)
    Springer
    Molecular genetics and genomics 217 (1989), S. 178-181 
    Details
    ISSN: 1617-4623
    Keywords: Chromosome partition ; parA ; gyrB ; psd
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A thermosensitive (ts) parA mutant, MFT110, of Escherichia coli carried at least two ts mutations. The major ts defect, resulting from a mutation mapped originally at 95 min and complemented by pLC8-47, was most probably due to psd. A plasmid carrying the 1.6 kb BamHI-PvuII fragment recloned from pLC8-47 complemented the major ts mutation in MFT110 and psd(ts) in two mutants, but did not correct the Par phenotype of MFT110. The second ts mutation was salt-repairable and mapped at 83 min close to recF and tnaA. This mutation was linked with the Par phenotype as shown unambiguously by 4′,6-diamidino-2-phenylindole stained nucleoids in parA mutant cells with the W3110 genetic background. Both salt-repairable ts and Par traits were corrected concomitantly by a plasmid carrying the chromosomal region solely for the gyrB gene. This strongly suggests that parA is an allele of gyrB.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330959
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  • 5
    Electronic Resource
    Electronic Resource
    Dispensability of either penicillin-binding protein -1a or -1b involved in the essential process for cell elongation in Escherichia coli (1985)
    Springer
    Molecular genetics and genomics 200 (1985), S. 272-277 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A strain of Escherichia coli lacking the entire ponB gene and a strain lacking the proximal part of the ponA gene were constructed by substitution with a drug resistance gene. These strains lost either penicillin-binding protein(PBP) -1b or -1a totally and their growth was apparently normal at 30°C and 42°C except that growth of the ponB deletion strain was poor on a nutrient agar plate containing no NaCl at 30°C as well as at 42°C. Transductional experiments to introduce the ponB deletion into the ponA deletion strain, and vice versa, showed that the ponA ponB double deletion was lethal unless the deletion was functionally compensated, e.g., by the presence of a plasmid carrying either gene. Thus, either PBP-1b (ponB) or PBP-1a (ponA), but not both, is dispensable for cell viability, at least under ordinary culture conditions. Transductional experiments also suggested that the γ component of PBP-1b or the PBP-1b lacking the C-terminal portion encoded in the distal region to the SphI site on the ponB was sufficient for supporting growth of the E. coli cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425435
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  • 6
    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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  • 7
    Electronic Resource
    Electronic Resource
    On the process of cellular division in Escherichia coli: Nucleotide sequence of the gene for penicillin-binding protein 3 (1983)
    Springer
    Molecular genetics and genomics 191 (1983), S. 1-9 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary We determined the nucleotide sequence of a DNA fragment containing the ftsI gene coding for the penicillin-binding protein 3 (PBP-3), an indispensable enzyme for cell division of Escherichia coli. The entire ftsI gene was within the 2.8 kilobase PvuII fragment derived from the chromosomal segment on pLC26-6 (Nishimura et al. 1977). The coding region for PBP-3 was identified by comparison with the N-terminal amino acid sequence of in vitro synthesized PBP-3. The structural gene for ftsI consisted of 1,764 base-pairs coding for a 588 amino acid residuepolypeptide with a molecular weight of 63,850. PBP-3 synthesized in vitro showed a lower mobility in SDS-gel electrophoresis than that of the authentic PBP-3, suggesting that the primary translation product of the ftsI gene may be processed to yield mature PBP-3.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00330881
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  • 8
    Electronic Resource
    Electronic Resource
    Gene fliA encodes an alternative sigma factor specific for flagellar operons in Salmonella typhimurium (1990)
    Springer
    Molecular genetics and genomics 221 (1990), S. 139-147 
    Details
    ISSN: 1617-4623
    Keywords: DNA sequence ; FliA purification ; Flagellar regulon ; Transcriptional activator ; Sigma factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Through genetic studies, the fliA gene product has been shown to regulate positively gene expression in late operons of the flagellar regulon in Salmonella typhimurium. In the present study, the fliA gene was cloned and sequenced. The fliA coding region consisted of 717 nucleotides beginning with the GTG initiation codon and the conserved sequence specific to promoters for flagellar operons was found to exist upstream of the coding region. The fliA gene product deduced from the nucleotide sequence was a protein with 239 amino acid residues and the calculated molecular mass was 27470 dalton. The deduced amino acid sequence was homologous with that of σ28, a flagellar specific sigma factor of Bacillus subtilis. The fliA gene product was identified as a protein of molecular mass 29 kDa in the in vitro transcription-translation system, while three proteins of 29 kDa, 31 kDa and 32 kDa were found in the products programmed by the fliA gene in minicells and in maxicells. The 29 kDa FHA protein was purified from the FliA overproducing strain which carried the ptac-fliA fusion. This protein activated the in vitro synthesis of flagellin, the fliC gene product. RNA polymerase containing the purified FliA protein was shown to transcribe the fliC gene. These results indicate that FliA protein functions as an alternative sigma factor specific for S. typhimurium flagellar operons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00261713
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