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  • 1
    Electronic Resource
    Electronic Resource
    RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits (1996)
    [s.l.] : Nature Publishing Group
    Nature 383 (1996), S. 172-175 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We initially examined the ability of recombinant His-tagged RGS1 (or His-tagged Erk2 as a negative control) to bind purified G-protein subunits in vitro. An interaction between RGS1 and Ga0 was detected, but was inefficient as most of the Ga subunits remained unbound (Fig. la). No interaction ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/383172a0
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  • 2
    Electronic Resource
    Electronic Resource
    Unaltered stability of newly synthesized RNA in strains of Escherichia coli missing a ribonuclease specific for double-stranded RNA (1975)
    Springer
    Molecular genetics and genomics 136 (1975), S. 317-326 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Paris of very closely related Escherichia coli strains were prepared, one having the wild-type allele for ribonuclease III, an enzyme which specifically degrades doublestranded RNA, and the other having a mutant RNase III allele. Growth and phage plating efficiency were compared in these strains. The RNase III+ strains grow better than the RNase III- strains and plate T7 and λ phage better, but T4 plates with the same efficiency on both strains. On the other hand, the half lives of newly synthesized RNA as well as of functional β-galactosidase mRNA are similar in both kind of strains. These two parameters, however, are significantly longer in both strains as compared to the original strain from which they were derived. Also, no difference in the differential induction of β-galactosidase was observed between such strains. Thus, we have to conclude that either ribonuclease III does not play a significant role in the functioning and stability of newly synthesized mRNA, or that enough enzymatic activity was left, residual RNase III or some other enzyme to deal with doublestranded regions in the message.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00341716
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  • 3
    Electronic Resource
    Electronic Resource
    Analysis of an Escherichia coli strain carrying physiologically compensating mutations one of which causes an altered ribonuclease III (1974)
    Springer
    Molecular genetics and genomics 132 (1974), S. 89-104 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A mutant of Escherichia coli, AB105, low in the level of ribonuclease III (an enzyme which degrades double-stranded RNA only), was obtained after treating cells of a ribonuclease I-free strain, A19, with nitrosoguanidine [Kindler, Kiel, and Hofschneider: Molec. gen. Genet. 126, 53–69 (1973)]. By a series of consecutive transductions, using a single E. coli strain, D10, related to the parental strain, as donor, we showed that strain AB105 is separated from strain A19 by at least seven mutations. In order to carry out these transductions, we made use of a number of phenotypic differences which distinguish strains A19 and AB105, such as poor growth on minimal medium or rich medium at any temperature, inability to utilize a variety of carbon sources, etc. After removing some of those mutations it became possible to transduce into such strains the RNase III+ allele from the donor strain D10. Pairs of RNase III+ and RNase III- strains, related one to the other by a single transduction were compared. T4 titers on both types of strains with the same efficiency, while T7 and λ titer better on RNase III+ strains. RNase III+ strains grow slightly better than RNase III- strains at all temperatures, however, at elevated temperatures RNase III+ strains unlike RNase III- strains fail to grow on minimal medium. Thus it seems that the mutation to RNase III- in strain AB105 compensates for some defect that does not permit such strains to grow on minimal medium at elevated temperatures. The enzyme seems to have an indispensible function in the cell but this function is not known yet.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00272175
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  • 4
    Electronic Resource
    Electronic Resource
    Consequences of losing ribonuclease III on theEscherichia coli cell (1976)
    Springer
    Molecular genetics and genomics 144 (1976), S. 185-190 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An isogenic pair ofEscherichia coli strains, one carrying anrnc + and the other anrnc − allele (a mutation which reduces the level of ribonuclease III), was compared. Thernc − strain fails to grow at very elevated temperatures (forE. coli) while thernc + strain does grow exponentially. Assaying the residual RNase III, like activity in extracts of thernc − strain at different pHs and at different temperatures suggested that this residual RNase III like activity is not due to RNase III. This raised the possibility that thernc − strain is devoid of any RNase III activity in the cell. Comparing the decay of newly synthesized RNA and functional decay of β-galactosidase mRNA in such strains revealed that in both strains these parameters proceed in similar rates, which suggests that RNase III is not involved in the metabolism of mRNA. During carbon starvation preexisting total RNA, as well as 23S and 16S rRNA, decay faster in thernc − strain, thus eliminating the possibility that RNase III is the endoribonuclease which initiates the decay of rRNA during starvation (Kaplan and Apirion, 1975a).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02428107
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  • 5
    Electronic Resource
    Electronic Resource
    A lethal mutation which affects the maturation of ribosomes (1976)
    Springer
    Molecular genetics and genomics 147 (1976), S. 29-37 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A temperature sensitive mutant of Escherichia coli which fails to recover from prolonged carbon starvation, was found to be irreversibly killed by exposure to a nonpermissive temperature (43°C), with a half-life of about half an hour. This bacteriocidal effect of the temperature could be reversed by a number of antibiotics which block protein synthesis but not by blocking DNA synthesis. At the nonpermissive temperature, RNA and the protein synthetic capacities decrease before the DNA synthetic capacity is decreased. Analysis of ribosomal proteins and methylation of them did not reveal any consistent differences between the parental and mutant strains. Analysis of the ribosomal RNA revealed that it is being synthesized in similar amounts as in the parental strain at the nonpermissive temperature, however, after chase its level is decreased. Moreover, the 17S precusor RNA is slow to mature to 16S rRNA in the mutant strain at the nonpermissive temperature. Thus, these studies suggest that the mutation studied here affects a late maturation step in the synthesis of the rRNA. Therefore the gene is designated rimH (for ribosomal modification). All the properties bestowed on the mutant strain are caused by a single pleiotropic mutation which maps at min 14 of the E. coli map. Three point transduction crosses suggest the order rimH, leuS, rna, lip. This gene maps outside the two known clusters for ribosomal structural genes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00337932
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  • 6
    Electronic Resource
    Electronic Resource
    Revertants from RNase III negative strains of Escherichia coli (1976)
    Springer
    Molecular genetics and genomics 149 (1976), S. 201-210 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary E. coli strains carrying the rnc-105 allele do not show any level of RNase III in extracts, grow slower than rnc + strains at temperatures up to 45°C and fail to grow at 45°C. Revertants which can grow at 45°C were isolated. The vast majority of them still do not grow as fast as rnc + strains and did not regain RNase III activity. The mutation(s) which caused them are suppressor mutations (physiological suppressors) which do not map in the immediate vicinity of the rnc gene. A few of the revertants regain normal growth, and contain normal levels of RNase III. They do not harbor the rnc-105 allele and therefore are considered to be true revertants. By using purines other than adenine it was possible to isolate rnc + pur - revertants from an rnc - pur - strain with relative ease. They behaved exactly like the true rnc + revertants isolated from rnc - strains at 45°C. A merodiploid strain which contains the rnc + gene on an episome behaves exactly like an rnc + strain with respect to growth and RNA metabolism, eventhough its specific RNase III activity is about 60% of that of an rnc + strain; thus the level of RNase III is not limiting in the cell. The rnc - strains show a characteristic pattern of transitory molecules, related to rRNA, 30S, 25S, “p23” and 18S, which are not observed in rnc + strains. This pattern is unchanged in rnc - strains and in the revertants which are still lacking RNase III, regardless of the temperature in which RNA synthesis was examined (30° to 45°C). On the other hand, in the rnc + strains as well as in the true revertants and the rnc +/rnc - merodiploid, the normal pattern of p16 and p23 is observed at all temperatures. These findings suggest that all the effects observed in RNase III- strains are due to pleiotropic effects of the rnc-105 allele, and that the enzyme RNase III is not essential for the viability of the E. coli cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00332890
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  • 7
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    Self cleavage of a precursor RNA from bacteriophage T4 (1984)
    Elsevier
    Details
    Publication Date: 1984-01-01
    Print ISSN: 0022-2836
    Electronic ISSN: 1089-8638
    Topics: Biology
    Published by Elsevier
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  • 8
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    A second gene which affects the RNA processing enzyme ribonuclease P ofEscherichia coli (1980)
    Wiley
    Details
    Publication Date: 1980-02-11
    Print ISSN: 0014-5793
    Electronic ISSN: 1873-3468
    Topics: Biology , Chemistry and Pharmacology
    Published by Wiley on behalf of Federation of European Biochemical Societies.
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  • 9
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    RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits (1996)
    Springer Nature
    Details
    Publication Date: 1996-09-01
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Springer Nature
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  • 10
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    Point mutations in a pBR322-based expression plasmid resulting in increased synthesis of bovine growth hormone in Escherichia coli (1990)
    Elsevier
    Details
    Publication Date: 1990-02-01
    Print ISSN: 0378-1119
    Electronic ISSN: 1879-0038
    Topics: Biology
    Published by Elsevier
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