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  • 1
    Electronic Resource
    Electronic Resource
    In vivo effect of inactivation of ribosome recycling factor – fate of ribosomes after unscheduled translation downstream of open reading frame (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 54 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The post-termination ribosomal complex is disassembled by ribosome recycling factor (RRF) and elongation factor G. Without RRF, the ribosome is not released from mRNA at the termination codon and reinitiates translation downstream. This is called unscheduled translation. Here, we show that at the non-permissive temperature of a temperature-sensitive RRF strain, RRF is lost quickly, and some ribosomes reach the 3′ end of mRNA. However, instead of accumulating at the 3′ end of mRNA, ribosomes are released as monosomes. Some ribosomes are transferred to transfer-messenger RNA from the 3′ end of mRNA. The monosomes thus produced are able to translate synthetic homopolymer but not natural mRNA with leader and canonical initiation signal. The pellet containing ribosomes appears to be responsible for rapid but reversible inhibition of most but not all of protein synthesis in vivo closely followed by decrease of cellular RNA and DNA synthesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04324.x
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  • 2
    Electronic Resource
    Electronic Resource
    Chloroplast gene organization deduced from complete sequence of liverwort Marchantia polymorpha chloroplast DNA (1986)
    [s.l.] : Nature Publishing Group
    Nature 322 (1986), S. 572-574 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] The genes encoding the chloroplast rRNAs (16S, 23S, 4.5S and 5S rRNAs) were localized by Southern hybridization with specific rRNA probes8"10. DNA sequences also confirmed the presence of the rRNA operons in both inverted repeat regions. Genes encoding tRNAs were localized using the Ti/f loop ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/322572a0
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  • 3
    Electronic Resource
    Electronic Resource
    Partial inhibition of protein synthesis accelerates the synthesis of porphyrin in heme-deficient mutants of Escherichia coli (1995)
    Springer
    Molecular genetics and genomics 249 (1995), S. 139-146 
    Details
    ISSN: 1617-4623
    Keywords: Glutamyl-tRNA reductase Peptidyltransferase ; Porphyrin ; Heme
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Mutants of Escherichia coli defective in the HemA protein grow extremely poorly as the result of heme deficiency. A novel hemA mutant was identified whose rate of growth was dramatically enhanced by addition to the medium of low concentrations of translational inhibitors, such as chloramphenicol and tetracycline. This mutant (H110) carries mutation at position 314 in the hemA gene, which resulted in diminished activity of the encoded protein. Restoration of growth of H110 upon addition of the drugs mentioned above was due to activation of the synthesis of porphyrin. However, this activation was not characteristic exclusively of cells with this mutant hemA gene since it was also observed in a heme-deficient strain bearing the wild-type hemA gene. The activation did not depend on the promoter activity of the hemA gene, as indicated by studies with fusion genes. It appears that partial inhibition of protein synthesis via inhibition of peptidyltransferase can promote the synthesis of porphyrin by providing an increased supply of Guamyl-tRNA for porphyrin synthesis. Glutamyl-tRNA is the common substrate for peptidyltransferase and HemA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00290359
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  • 4
    Electronic Resource
    Electronic Resource
    Genes and sites involved in replication and incompatibility of an R100 plasmid derivative based on nucleotide sequence analysis (1980)
    Springer
    Molecular genetics and genomics 179 (1980), S. 527-537 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The nucleotide sequence of the entire region required for autonomous replication and incompatibility of an R100 plasmid derivative, pSM1, has been determined. This region includes the replication region and all plasmid encoded information required for replication. Numerous reading frames for possible proteins can be found in this region. The existence of one of these proteins called RepA1 (285 amino acids; 33,000 daltons) which is encoded within the region known by cloning analysis to be required for replication is supported by several lines of evidence. These include an examination of the characteristic sequences on the proximal and distal ends of the coding region, a comparison of the sequence of the replication regions of pSM1 and the highly related R1 plasmid derivative Rsc13 as well as other biochemical and genetic evidence. The existence of two other proteins, RepA3 (64 amino acids; 7000 daltons) and RepA2 (103 amino acids; 11,400 daltons) is also consistent with most of the criteria mentioned above. However, the region encoding RepA3, which by cloning analysis is within the region responsible for both replication and incompatibility, has never been demonstrated to produce a 7,000 dalton polypeptide. Since a large secondary structure can be constructed in this region, it is possible that the region contains structure or other information that is responsible for incompatibility. RepA2, encoded entirely within the region identified by cloning analysis to be responsible for incompatibility but not for replication can be visualized in vivo and in vitro. However, the nucleotide sequence of the region encoding RepA2 is completely different in mutually incompatible plasmid derivatives of R1 and R100. It is therefore unlikely that RepA2 plays a major role in incompatibility. Thus, we predict that RepA1 is required to initiate DNA synthesis at the replication origin and that the region proximal to RepA1 either encodes a gene product or structure information that is responsible for incompatibility.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00271742
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  • 5
    Electronic Resource
    Electronic Resource
    Lambda phage mutants insensitive to temperature-sensitive repressor (1969)
    Springer
    Molecular genetics and genomics 104 (1969), S. 51-58 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Weak-virulent mutants of temperate coli-phage λ were isolated which can grow on the λCIts lysogen producing a temperature-sensitive repressor but which cannot grow on the wild type λ lysogen producing a normal repressor. Genetic analysis on the mutants shows that their weak-virulence is attributable to two mutations, one (virL) in the region between sus N213 and c 47 and the other (virR) in the region between c 1 and sus O8. Both mutations are located within the region of non-homology between λ and λimm 434 phages. True virulent mutants which can grow on the wild type λ lysogen can be obtained easily from the weak-virulent mutant by an additional mutation, virC in a region very close to virR. The virulent mutants obtained are similar to the classical λvir mutant (Jacob and Wollman, 1954). The virL and virR mutations are probably operator mutations which render the genome insensitive to the λ repressor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00277362
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  • 6
    Electronic Resource
    Electronic Resource
    Mutant of the glutamine transfer RNA gene as UGA suppressor in Escherichia coli (1990)
    Springer
    Molecular genetics and genomics 223 (1990), S. 433-437 
    Details
    ISSN: 1617-4623
    Keywords: UGA suppressor ; tRNA 2 Gln gene ; Lethal effect ; Escherichia coli
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A UGA suppressor derived from a glutamine tRNA gene of Escherichia coli K 12 was isolated and characterized. Phages carrying the suppressor su+2UGA could be obtained only from a hybrid transducing phage, h 80 cI 857psu +2oc, but not from the original transducing phage λcI 857psu +2oc. By DNA sequence analysis, it was found that the su +2 UGA suppressor obtained has two mutations; one is in the anticodon (TTA→TCA), as expected, and the other (C→T) is at the 7th position from the 3′ end of tRNA 2 Gln . The significance of these mutations and the lethal effect on phage λ of the increased amounts of UGA suppressor tRNAs are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00264450
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  • 7
    Electronic Resource
    Electronic Resource
    Genetic analysis of functional connectivity between substrate recognition domains of Escherichia coli glutaminyl-tRNA synthetase (1996)
    Springer
    Molecular genetics and genomics 252 (1996), S. 717-722 
    Details
    ISSN: 1617-4623
    Keywords: Key words Glutaminyl-tRNA synthetase ; Temperature sensitivity ; Substrate specificity ; Aminoacylation ; Suppressor tRNA
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  It has previously been shown that the single mutation E222K in glutaminyl-tRNA synthetase (GlnRS) confers a temperature-sensitive phenotype on Escherichia coli. Here we report the isolation of a pseudorevertant of this mutation, E222K/C171G, which was subsequently employed to investigate the role of these residues in substrate discrimination. The three-dimensional structure of the tRNAGln :  GlnRS : ATP ternary complex revealed that both E222 and C171 are close to regions of the protein involved in interactions with both the acceptor stem and the 3′ end of tRNAGln. The potential involvement of E222 and C171 in these interactions was confirmed by the observation that GlnRS-E222K was able to mischarge supF tRNATyr considerably more efficiently than the wild-type enzyme, whereas GlnRS-E222K/C171G could not. These differences in substrate specificity also extended to anticodon recognition, with the double mutant able to distinguish supE tRNAGln CUA from tRNAGln 2 considerably more efficiently than GlnRS E222K. Furthermore, GlnRS-E222K was found to have a 15-fold higher Km for glutamine than the wild-type enzyme, whereas the double mutant only showed a 7-fold increase. These results indicate that the C171G mutation improves both substrate discrimination and recognition at three domains in GlnRS-E222K, confirming recent proposals that there are extensive interactions between the active site and regions of the enzyme involved in tRNA binding.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02173978
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  • 8
    Electronic Resource
    Electronic Resource
    Polarity effect on Φ80 late gene expression caused by insertion of su+3-transducing fragment (1977)
    Springer
    Molecular genetics and genomics 155 (1977), S. 139-143 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary During vegetative growth, the su+3-transducing phage of Φ80 segregates progeny phage which has lost the su+3-transducing fragment. Average burst size of the transducing phage is less than one tenth that of the segregant. Burst size of the transducing phage was recovered to the normal level when segregant-type phage was co-infected as a helper. We suspected that the maturation process was partially inhibited by a polar effect caused by insertion of the su+3-transducing fragment into the continuity of Φ80 late genes. To determine which gene expressions are partially inhibited in the transducing phage, various amber mutants were used as the helper phage and burst size of the transduzing phage was measured in the system where excision of the transducing fragment was inhibited. The results indicated that gene expression of a group of genes 4 to 13 was reduced in the transducing phage, while that of a group of genes 1, 2 and 3 was not. The specificity of partial inhibition of gene function agrees well with the results of physical mapping of the transducing fragment; that is, the fragment was inserted within the region of gene 4 by heteroduplex analysis (Yamagishi et al., 1976a).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00393152
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  • 9
    Electronic Resource
    Electronic Resource
    Characterization of the dnaA gene carried by lambda transducing phage (1980)
    Springer
    Molecular genetics and genomics 180 (1980), S. 235-247 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Specialized transducing phages λdnaA were obtained by inducing lysogens in which λtna was integrated at the tnaA region of the Escherichia coli chromosome; the tnA region is located in the vicinity of the dnaA gene. The dnaA - deletion derivatives of λdnaA were isolated from the lysate of λdnaA grown on bacteria carrying a transposon Tn3. The structures of various transducing phages thus obtained were determined by heteroduplex DNA mapping. From these results, the transducing fragment of 13.8-kb-long was divided into nine domains. Upon infection of UV-irradiated cells with the phage, production of polypeptides of 49 kD and 42 kD was specifically associated with infections by the dnaA and recF transducing phages. Polypeptides of 49 kD and 42 kD appeared to be coded for by dnaA and recF genes, respectively. The dnaA gene was assigned to the region of 2.8-kb-long which extends by 2.4 kb in the counterclockwise direction on the E. coli genetic map and 0.4 kb in the opposite direction, as measured from the nearest HindIII site close to the tnaA gene. The recF gene was also discovered to lie very close to dnaA in the order of tnaA-dnaA-recF. Merogenotes heterozygous for the dnaA gene were constructed by introducing F′100-12 carrying λdnaA into the recipients with different mutations at or near dnaA. For combinations, F′(λdnaA +)/dnaA46 and F′(λdna +)/dna-83, dnaA + was trans-dominant, whereas the dnaA + was recessive for F′(λdnaA +)/dna-5. For F′(λdnaA +)/dna-167, the result of the transdominance test was affected by the growth media employed; dnaA + was dominant on a λ-broth plate, and dna-167 was dominant on an M9-minimal plate. Thus, transdominance of dnaA + in heterozygotes is affected by difference in mutations and growth media.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425835
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  • 10
    Electronic Resource
    Electronic Resource
    The third member of the hemA gene family encoding glutamyl-tRNA reductase is primarily expressed in roots in Hordeum vulgare (1997)
    Springer
    Photosynthesis research 53 (1997), S. 161-171 
    Details
    ISSN: 1573-5079
    Keywords: chlorophyll ; heme ; Hordeum vulgare ; glutamyl-tRNA reductase ; hemA ; 5-aminolevulinate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Accumulation of chlorophylls and heme is primarily controlled at the level of 5-aminolevulinate (ALA) synthesis in higher plants. ALA is formed from glutamate in three enzymatic steps in plants. Among them, the reduction of glutamyl-tRNAGluto glutamate-1-semialdehyde (GSA) is likely to be a regulatory point of ALA synthesis. This reaction is catalyzed by glutamyl-tRNA reductase (GTR), which is encoded by a hemA gene. We have isolated a novel isoform of a hemA cDNA clone from barley (Hordeum vulgare) that is the third member of the hemA gene family. mRNA of this isoform is accumulated primarily in roots, suggesting that the isoform is regulated in an organ-specific manner by the demand for heme synthesis rather than chlorophyll. Phylogenetic analysis was done using the deduced amino acid sequences of hemA isoforms from barley, cucumber and Arabidopsis thaliana. The results indicate that the existing gene families in these plants arose after the divergence of monocotyledonous and dicotyledonous plants.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005809800959
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