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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 25 (1986), S. 1170-1175 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 36 (1993), S. 555-567 
    ISSN: 1432-1432
    Keywords: Ornithine decarboxylase ; mRNA evolution ; Episodic evolution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ornithine decarboxylase (ODC) is the first enzyme in the polyamine biosynthetic pathway. We have studied the evolutionary history of the mammalian ODC mRNA, focusing on the rate of accumulation of sequence divergence within specific subregions of the molecule. The phylogenetic relationships among the mRNAs from several mammalian species, including two mouse species, rat, hamster, and human, were determined based upon the numbers of synonymous substitutions in pair-wise comparisons of mRNA coding regions. The separation times for the mRNAs were very similar to those for the corresponding species, suggesting that ODC is encoded by orthologous genes in the different species. Analysis of divergence patterns in four subregions, or domains, of the mRNA (the 5′untranslated region, the coding region, and two domains of the 3′-untranslated region) showed that the domains have evolved in a noncoordinate fashion. Furthermore, evolution of each subregion has been episodic, with periods of both rapid and slow sequence divergence. We suggest that the episodic pattern of ODC mRNA evolution may indicate the existence of selection pressures that were exerted in a time- and domain-specific manner during mammalian speciation.
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 48 (1999), S. 252-252 
    ISSN: 1432-1432
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of molecular evolution 46 (1998), S. 639-648 
    ISSN: 1432-1432
    Keywords: Key words: Transcription — Promoter — Regulatory element —Mus genus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. Previously, we identified evolutionarily derived changes in the pattern of nuclear factor binding to overlapping sites (termed A, B, and C, in proximal to distal order) within the promoter region of the murine D7Rp2e gene. In Mus domesticus, strong binding occurs at site B, with weak binding at sites A and C; in M. pahari, strong binding is observed at sites A and C, with weak binding at site B. The M. pahari-specific occupancy pattern is associated with repression of transcription. Presently, we have identified two interspecies changes, a single A → G substitution within site B and a 7-bp indel within site C, that are primary determinants of the interspecies differences. These mutations alter both the pattern of binding site occupancy and the ability to repress transcription. The results are discussed in terms of a model involving a dynamic equilibrium between states of binding site occupancy, the nature of which can be modified during evolution.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    [s.l.] : Nature Publishing Group
    Nature 282 (1979), S. 314-316 
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] A genetic complex, termed [Bgl], mapping near the Mod-l locus on chromosome 9, contains within it elements governing the structure, development and rate of synthesis of /3-galac-tosidase4'9"15. The structural gene Bgl-e is defined by an electrophoretic polymorphism which affects the enzyme in all ...
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 15-23 
    ISSN: 1573-4927
    Keywords: major urinary proteins ; genetic variation ; mouse genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A two- to fourfold difference in the relative rate of total major urinary protein (MUP) synthesis between C57BL/6J and C3H/HeJ female mice has been analyzed at the genetic and molecular levels. The C57BL/6J phenotype is dominant in F1 female progeny of a cross between the two strains. Quantitation of MUP mRNA levels indicates that the rate of synthesis variation does not reflect a change in the concentration of total MUP mRNA. In recombinant inbred strains derived from C57BL/6J and C3H/HeJ progenitors, the rate of synthesis difference segregates as a single genetic determinant that is not linked to the Mup-a locus on chromosome 4. The results suggest an unlinked locus that acts to alter total MUP synthesis without altering total MUP mRNA levels. Two models are proposed to describe the action of this locus, both of which imply some sort of posttranscriptional control of MUP synthesis.
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 21 (1983), S. 15-23 
    ISSN: 1573-4927
    Keywords: major urinary proteins ; genetic variation ; mouse genetics
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A two- to fourfold difference in the relative rate of total major urinary protein (MUP) synthesis between C57BL/6J and C3H/HeJ female mice has been analyzed at the genetic and molecular levels. The C57BL/6J phenotype is dominant in F1 female progeny of a cross between the two strains. Quantitation of MUP mRNA levels indicates that the rate of synthesis variation does not reflect a change in the concentration of total MUP mRNA. In recombinant inbred strains derived from C57BL/6J and C3H/HeJ progenitors, the rate of synthesis difference segregates as a single genetic determinant that is not linked to theMup-a locus on chromosome 4. The results suggest an unlinked locus that acts to alter total MUP synthesis without altering total MUP mRNA levels. Two models are proposed to describe the action of this locus, both of which imply some sort of posttranscriptional control of MUP synthesis.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 27 (1989), S. 745-753 
    ISSN: 1573-4927
    Keywords: mouse ; ornithine decarboxylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Ornithine decarboxylase (ODC), the first enzyme in the polyamine biosynthetic pathway, is encoded by at least one member of a multi-gene family in the mouse. Analysis of a polymorphism in ODC structure in recombinant inbred strains has enabled assigning a functional ODC structural gene (Odc) to the proximal region of mouse chromosome 12 betweenApob andEs25. Linkage ofOdc toApob andAh is conserved in the mouse and human genomes.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 19 (1981), S. 1261-1273 
    ISSN: 1573-4927
    Keywords: major urinary proteins ; rate of synthesis ; androgen regulation ; mouse liver
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract By labeling liver protein in vivo with [3H]leucine, the relative biosynthetic rate has been measured for the major urinary proteins (MUPs), three closely related, androgen-regulated proteins that are synthesized in mouse liver, secreted into the bloodstream, and excreted into the urine. In livers from females of strain C57BL/6J, total MUP synthesis represents about 0.6–0.9% of the total protein synthesis; in males and testosterone-treated females of the same strain, synthesis increases to about 3.5–4.0% of the total. This 4-to 6-fold induction of total MUP synthesis is similar to the androgen-mediated increase in MUP-specific messenger RNA reported by others, and indicates that the previously observed 20- to 25-fold induction of total MUP excretion into urine is generated partly at the posttranslational level. By measuring the ratio of synthesis of the individual MUPs, it was determined that the testosterone-mediated change in the relative levels of the MUPs in urine reflects a similar change in the pattern of MUP synthesis, indicating that the posttranslational processes operate on the quantity, and not the nature, of MUPs excreted. A survey of seven inbred mouse strains revealed polymorphism for the rate of total MUP synthesis in untreated females. Two classes could be distinguished on the basis of a 3- to 5-fold difference in the rate. This variation does not correlate with variation at Mup-a, a locus that controls the ratio of the three MUPs in urine from androgen-induced mice. These findings are consistent with the notion that MUP expression is controlled by a variety of independently assorting genes.
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  • 10
    Electronic Resource
    Electronic Resource
    Springer
    Biochemical genetics 16 (1978), S. 1007-1014 
    ISSN: 1573-4927
    Keywords: β-galactosidase ; mouse ; structural variation ; thermal stability ; electrophoretic mobility
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract We have examined the relationships between the genetic determinants for mouse β-galactosidase heat stability and electrophoretic mobility, in order to clarify previous reports indicating that a variation for enzyme heat stability is restricted to kidney while that for electrophoretic mobility is expressed in all tissues. We find that the two phenotypes show concordant strain distributions and cosegregate in genetic crosses. In contrast to a previous report, the thermal stability variation is expressed in all tissues, although the absolute rate of enzyme inactivation is tissue specific. The evidence supports the notion that a single β-galactosidase structural locus is expressed in all tissues and that the differences in enzyme stability between tissues results from posttranslational enzyme modification.
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