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  • 1
    Electronic Resource
    Electronic Resource
    Transcriptional activation of immunoglobulin α heavy-chain genes by translocation of the c-myc oncogene (1983)
    [s.l.] : Nature Publishing Group
    Nature 305 (1983), S. 443-446 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Dot-blot analysis of cytoplasmic RNA was used as an initial test for Ca-gene transcription in three IgG-producing myeloma lines. Two of the cell lines, MPC 11 (IgG2b) and MOPC 21 (IgGl), contain Ca genes in the germ-line configuration, while one of the Ca alleles in HOPC 1 (IgG2a) is rearranged to ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/305443a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    A mutant rho ATPase from Escherichia coli that is temperature-sensitive in the presence of RNA (1981)
    Springer
    Molecular genetics and genomics 181 (1981), S. 367-372 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Escherichia coli mutant rho-115 suppresses lac operon polarity conferred by the lacZ::IS1 insertion MS319. The ATPase activity of purified rho-115 protein was maximal at 40°C, in contrast to 45°C for rho +. At higher temperatures (50°C, 55°C), the fractions of activities at maximal temperature were consistently lower for rho-115 compared to rho +. The 30-minute time course of rho-115 ATP hydrolysis was linear at 37°C but at 45°C the linear kinetics of hydrolysis reached a plateau between 10 and 15 minutes. The 30-minute time courses for rho + were linear at both 37°C and 45°C. The rho-115 and rho + ATPase activities were equally heat-stable during preincubation at 45°C in buffer. Inclusion of ATP during preincubation protected these rho proteins from inactivation to the same extent. The presence of polyC during preincubation protected rho - activity but produced substantial inactivation of rho-115 ATPase. The presence of polyU during preincubation gave similar results. Concentrations of polyC between 625 ng/ml and 100 μg/ml yielded the same extent of rho-115 ATPase inactivation during preincubation at 45°C. Thermal inactivation of rho-115 ATPase by polyC was halted by shifting preincubation temperature from 45°C to 35°C, indicating that polyC-induced destabilization of rho-115 was irreversible.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00425613
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  • 3
    Electronic Resource
    Electronic Resource
    Temperature-sensitive mutant rho-115 rho-RNA binary complexes, and stabilization by substrates and analogues (1982)
    Springer
    Molecular genetics and genomics 187 (1982), S. 330-334 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary To determine the molecular basis for the temperature-sensitivity of pure rho RNA-dependent ATPase from Escherichia coli mutant rho-115 cells, we investigated mutant rho binding to [3H] polyC as measured by retention on nitrocellulose filters. Complexes of wild-type rho and polyC incubated at 37°C and 45°C were similarly stable. At 37°C mutant rho-polyC binary complexes were inactivated at a slightly faster rate than complexes with wild-type rho. Upon shift to 45°C the quantity of rho-115 bound to polyC declined immediately, resulting in one-fifth of the quantity of complexes observed at 37°C. Shift back to 37°C restored the level of observed complexes by two-fold. The inclusion of ATP or the analogue β-γ methylene ATP during 45°C incubation resulted in stable mutant rho-polyC complexes. The hydrolysis product ADP was also effective in stabilizing binary complexes at 45°C but this effect was observed with an order of magnitude more ADP than ATP. Adenine, adenosine, AMP or Pi had no stabilizing effect. We conclude that the mutant rho-115 protein exhibits a structural instability as a result of binding RNA. Furthermore ATP confers a wild-type phenotype upon rho-115 protein, probably as a result of conformational change due to binding of this compound. The effect of ATP on the stability of mutant rho-polyC binary complexes supports the model of ATP modulation of rho-RNA interaction proposed by Galluppi and Richardson (1980).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00331139
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