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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 197 (1984), S. 175-181 
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Discrepancies between our mapping data concerning the cdd and gat marker of Escherichia coli and data obtained by Josephsen et al. (1983) as well as with the current linkage map of Escherichia coli (Bachmann 1983) led us to reinvestigate the mapping of markers in the gyrA-his region by P1 transduction. In addition, we isolated Hfr strains by integrating the temperature-sensitive F'ts114 lac + episome via lac homology of cir'lacZ and mgl'lacZ fusions into the chromosome. From the results of the P1 transductions and using these Hfr strains as donors in crosses it became clear that the transcription of cir and mgl is the same and counterclockwise on the chromosome, with cdd and gat as the counterclockwise markers to mgl and cir. We conclude that our previously published sequence of markers was incorrect and is in fact inverted. The present data indicate the following sequence of markers in clockwise order: his gat cdd mgl cir fpk gyrA.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: Cell morphology ; DNA topology ; Gene expression ; Gene mapping ; Osmoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A class of trans-acting mutations, which alter the osmoregulated expression of the Escherichia coli proU operon, maps at 27 min on the chromosome in a locus we have called osmZ. Mutations in osmZ are allelic to bglY, pilG and virR, affect gene expression, increase the frequency of the site-specific DNA inversion mediating fimbrial phase variation, stimulate the formation of deletions, and influence in vivo supercoiling of reporter plasmids. We have cloned the osmZ + gene, mapped it at 1307 kb of the E. coli restriction map, identified its gene product as a 16 kDa protein, and determined the nucleotide sequence of the osmZ + gene. The deduced amino acid sequence for OsmZ predicts a protein of 137 amino acid residues with a calculated molecular weight of 15 530. The primary sequence of OsmZ is identical to that of H-NS (H1a), a DNA-binding protein that affects DNA topology and is known to be associated with the bacterial nucleoid. Thus, osmZ is the structural gene for the H-NS (H1a) protein. The nucleotide sequence of osmZ is almost identical to that of hns; however, hns was incorrectly located at 6.1 min on the E. coli linkage map. Increased osmZ gene dosage leads to cell filament formation, altered gene expression, and reduced frequency of fimbrial phase variation. Our results suggest that the nucleoid-associated DNA-binding protein H-NS (H1a) plays a critical role in gene expression and in determining the structure of the genetic material.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 221 (1990), S. 491-494 
    ISSN: 1617-4623
    Keywords: Tsx ; Outer membrane ; Colicin K ; Bacteriophages ; Nucleoside uptake
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The tsx-206 allele encodes an altered Tsx protein, Tsx-206, that can no longer function as the T6 receptor. We show here that this allele also confers resistance to the Tsx-specific phages III, H3, H8, K9, K18 and Oxl but not to colicin K. The Tsx-206 protein still mediates the efficient permeation of deoxyadenosine across the outer membrane at low substrate concentration. A host-range mutant of phage T6, T6h3.1, was isolated which can use both the Tsx-206 and the Tsx wild-type protein as its receptor. Cloning and DNA sequence analysis of the tsx-206 allele showed that the phage resistant phenotype was associated with an Asn to Tyr substitution at position 254 of the 272-residue Tsx protein.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1617-4623
    Keywords: Osmoregulation ; Periplasmic protein ; Signal sequence ; phoA fusions
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary ThetreA gene ofEscherichia coli K12 codes for a periplasmic trehalase that is induced by growth at high osmolarity. The position oftreA within a cloned chromosomal DNA fragment was identified by subcloning of restriction fragments and analysis of the gene product in minicells. The nucleotide sequence of thetreA coding region as well as its upstream control region was determined. ThetreA gene consists of 1695 bp encoding 565 amino acids. The amino-terminus of the mature trehalase was found to begin with the amino acid Glu at position 31 of the open reading frame. The first 30 amino acids resemble a typical signal sequence, consistent with trehalase being a secreted periplasmic enzyme. Two previously isolatedphoA fusions to theosmA gene were transferred by homologous recombination on to atreA-containing plasmid and found to be withintreA. Analysis of the hybrid genes and their gene products aided the localization oftreA and the determination of its direction of transcription within the cloned chromosomal segment. ThetreA-phoA fusions encoded hybrid proteins which could be found in the periplasm. We found that at high osmolarity the normal pathway for the uptake and utilization of trehalose is blocked. Therefore, the function of the periplasmic trehalase is to provide the cell with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system.
    Type of Medium: Electronic Resource
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  • 5
    Publication Date: 1990-01-01
    Print ISSN: 0378-1119
    Electronic ISSN: 1879-0038
    Topics: Biology
    Published by Elsevier
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