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  • 1
    ISSN: 1574-6968
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: To understand the nature and function of bacterial biofilm and the process of its formation, we have performed systematic screening of a complete set of Escherichia coli genes/open reading frames (ORFs) to identify those that affect biofilm development upon over-expression. In contrast to the biofilm of strain AG1 used as a control, some of the genes/ORFs when over-expressed led to the formation of an abnormal biofilm such as thin, mat-like, filamentous or one easily detaching from various surfaces. Disruptants of selected genes were constructed in order to clarify their roles in the different stages of biofilm formation. Our results suggest that diverse metabolic pathways contribute to the development of biofilm.
    Materialart: Digitale Medien
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  • 2
    ISSN: 1432-0983
    Schlagwort(e): Saccharomyces cerevisiae ; Nuclear gene ; Mitochondria ; Mitochondrial ribosomal protein
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The nuclear gene MRP-L13 of Saccharomyces cerevisiae, which codes for the mitochondrial ribosomal protein YmL13, has been cloned and characterized. It is a single-copy gene residing on chromosome XI. Its nucleotide sequence was found to be identical to that of the previously reported ORF YK105. A comparison of the predicted protein sequence of the MRP-L13 gene product and the actual N-terminal amino-acid sequence of the isolated YmL13 protein indicated that the mature protein is preceded by a mitochondrial signal peptide of 86 amino-acid residues, which is the longest among all known mitochondrial ribosomal proteins of S. cerevisiae. No sequence similarity was found to any other ribosomal protein in the current databases. The transcription of MRP-L13 was found to be repressed in the presence of glucose. Its protein product is not strictly essential for mitochondrial functions, but disruption of the gene by insertion of LEU2 noticeably affected cellular growth on non-fermentable carbon sources.
    Materialart: Digitale Medien
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  • 3
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Materialart: Digitale Medien
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  • 4
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 179 (1980), S. 311-317 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Temperature-sensitive mutants harbouring alterations in ribosomal proteins L28 and L33 have been isolated and used in mapping the genes coding for the two proteins. It was found that they mapped very close to each other and near pyrE at 80.7 min on the E. coli genetic map. The genes affected by the mutations have been concluded to be the structural genes for proteins L28 (rpmB) and L33 (rpmG) by constructing merodiploids heterozygous for pyrE and for the two ribosomal proteins. Various transduction studies with P1kc phages indicate the gene order in this region to be (rpmB, rpmG)-pyrE-spoT-gltC.
    Materialart: Digitale Medien
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  • 5
    ISSN: 1617-4623
    Schlagwort(e): Escherichia coli ; Ribosomal protein S6 ; Addition of glutamic acid residues ; Cloning and sequencing
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Ribosomal protein S6 of wild-type strains ofEscherichia coli contains up to six glutamic acid residues at its C-terminus. The first two residues are encoded by the structural gene for this protein (rpsF) and the rest are added post-translationally. Mutants deficient in this modification were isolated and characterized genetically and biochemically. The S6 protein in these mutants appeared to contain only two glutamic acid residues at the C-terminus as expected. The mutated gene was termedrimK and was mapped at 18.7 min betweencmlA andaroA. TherimK gene was cloned into a cosmid vector and its nucleotide sequence determined. Analysis of the transcriptional and translational products of this gene indicates that it encodes a protein with an Mr of 31.5 kDa and that it forms an operon with a gene encoding a 24 kDa protein. AnrpsF mutant containing a Glu to Lys replacement in the second residue from the C-terminus of protein S6 was isolated. The S6 protein of this mutant was apparently inaccessible to the RimK modification system. This indicates that the RimK modification system requires the wild-type amino acid sequence at least in the C-terminal region of ribosomal protein S6.
    Materialart: Digitale Medien
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  • 6
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 153 (1977), S. 115-120 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A mutant of E. coli selected for temperaturesensitive growth on rich medium harbored an altered ribosomal protein S6 (Isono et al., 1976). This mutant was found to possess at least two mutations, one being responsible for the temperature-sensitivity and the other for the S6 alteration. Crosses with various Hfr strains as well as transductions with P lkc revealed that the former mutation mapped at 98 min and the latter at 97 min. Furthermore, recA derivatives of this mutant heteromerodiploid for this region possessed both the wild type and the mutant forms of S6. Thus it was established that the gene at 97 min was indeed the structural gene for protein S6 (rpsF) and not a gene modifying it.
    Materialart: Digitale Medien
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  • 7
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 158 (1977), S. 149-155 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary A temperature-sensitive mutant derived from an E. coli K12 strain, PA3092, was found to have an alteration in the ribosomal protein L19 (Isono et al., 1977). This mutant is a double mutant with a temperature-sensitivity mutation and a mutation leading to the structural alteration of L19 protein. Crosses with various Hfr strains and transductions with P1kc have revealed that the latter mutation maps at 56.4 min, between pheA and alaS. From the fact that two other mutations causing different types of alterations in L19 protein also map at this locus, the gene affected by these mutations was concluded to be the structural gene for the ribosomal protein L19 (rplS).
    Materialart: Digitale Medien
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  • 8
    Digitale Medien
    Digitale Medien
    Springer
    Molecular genetics and genomics 180 (1980), S. 343-349 
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary Specialized transducing λ phages have been isolated which carry the regions of the Escherichia coli chromosome containing the gene or gene-clusters for ribosomal proteins (r-proteins) S 1, S 6-S 18-L 9, S 16-L 19, and L 28-L 33. To investigate whether these phages also carry the genes for r-proteins S 9, L 13, L 20, L 31, and L 34 whose gene locations are not known, cells irradiated with UV light were infected with these phages and the r-proteins synthesized were analyzed by two-dimensional gel electrophoresis. However, no synthesis of these r-proteins was stimulated, indicating that their genes are not located in the neighborhood of any of the above-mentioned genes or gene clusters. It was found that proteins S 6 and S 18 synthesized in the cells irradiated with UV light were not modified under these conditions in which no concomitant ribosome assembly took place.
    Materialart: Digitale Medien
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  • 9
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary The genes for the ribosomal proteins S9 (rpsI) and L13 (rplM) of Escherichia coli have been cloned into a λ phage vector termed L47.1. The two genes were identified by infecting UV-light irradiated cells with the resultant phages and analyzing the protein products by two-dimensional gel electrophoresis. Suitable DNA fragments of the isolate were cloned subsequently into M13 phage vectors and their nucleotide sequence was determined by the dideoxy method. It is evident that the two genes form a transcriptional unit, the rplM gene being promoter-proximal. There is a typical signal sequence for transcriptional termination after the rpsI gene. The codon usage pattern in the two genes is similar to other ribosomal protein genes of E. coli.
    Materialart: Digitale Medien
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  • 10
    ISSN: 1617-4623
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Summary An Escherichia coli mutant harbouring altered ribosomal protein L32 has been isolated and genetically characterized. The mutation leading to this alteration (rpmF) and the temperature-sensitive mutation (ts-1517) present in the same strain were found to map near pyrC (23.4 min), being cotransducible not only with pyrC but also with fabD, flaT and purB in P1 phage mediated transductions. Furthermore, we found that the gene rimJ, which encodes an enzyme that acetylates the N-terminal alanine of protein S5 and the temperature-sensitive mutation, ts-386, present in the rimJ mutant strain (Cumberlidge and Isono 1979) also mapped in this region. Thus, the order of genes is deduced to be: ts-386-pyrC-ts-1517-rimJ-flaT-fabD-rpmF-purB.
    Materialart: Digitale Medien
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