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Related Experiment Videos

Poly(A) polymerase in quail oviduct. Changes during estrogen induction.

W E Müller, A Totsuka, M Kroll

    Biochimica Et Biophysica Acta
    |March 10, 1975
    PubMed
    Summary

    A purified nuclear poly(A) polymerase from quail oviducts specifically synthesizes poly(A) chains. Enzyme activity is unaffected by estrogen stimulation, but poly(A) degradation decreases.

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Enzymology

    Background:

    • Nuclear poly(A) polymerase plays a crucial role in mRNA processing.
    • Understanding its regulation is key to comprehending gene expression control.

    Purpose of the Study:

    • To isolate and characterize a nuclear poly(A) polymerase from quail oviducts.
    • To investigate the enzyme's properties and its regulation by estrogen.

    Main Methods:

    • Purification of nuclear poly(A) polymerase from quail oviducts.
    • Enzyme activity assays using ATP and polynucleotide primers.
    • Analysis of enzyme kinetics and inhibition by analogues.
    • Hormonal stimulation studies with diethylstilbestrol.

    Main Results:

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    • A highly purified nuclear poly(A) polymerase was obtained, dependent on ATP and Mg2+.
    • The enzyme synthesized poly(A) chains up to 60 AMP residues on a polynucleotide primer.
    • Poly(A) polymerase activity was not altered by estrogen stimulation, but poly(A) degrading enzyme activity was reduced.

    Conclusions:

    • The characterized poly(A) polymerase is distinct from RNA polymerases.
    • Estrogen treatment downregulates poly(A) degradation rather than upregulating poly(A) synthesis in quail oviducts.