The biochemical basis of an all-or-none cell fate switch in xenopus oocytes

Science

Volumn 280, Issue 5365, 1998, Pages 895-898

  Ferrell Jr , James E ^a   Machleder, Eric M ^a  

^a STANFORD UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROGESTERONE;

ANIMAL CELL; ARTICLE; CELL CYCLE; CELL MATURATION; NONHUMAN; OOCYTE; POSITIVE FEEDBACK; PRIORITY JOURNAL; XENOPUS LAEVIS;

ANIMALS; CARRIER PROTEINS; CELL CYCLE; CYCLOHEXIMIDE; ENZYME ACTIVATION; FEEDBACK; KINETICS; MITOGEN-ACTIVATED PROTEIN KINASE 1; OOCYTES; PHOSPHORYLATION; PROGESTERONE; PROTEIN SYNTHESIS INHIBITORS; PROTO-ONCOGENE PROTEINS C-MOS; RECOMBINANT FUSION PROTEINS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0032496358     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.280.5365.895     Document Type: Article

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22. 4, 5 mM Hepes (pH 7.8) [R. A. Wallace, D. W. Jared, J. N. Dumont, M. W. Sega, J. Exp Zool. 184, 321 (1973)]}. Oocytes were treated with progesterone or microinjected with purified recombinant malE-Mos, incubated for 8 to 10 hours, and then collected individually and frozen on dry ice. Individual oocytes were lysed by the addition of ice cold lysis buffer (50 to 100 μl) [100 mM NaCl, 50 mM β-glycerolphosphate (pH 7.4), 10 mM EDTA, 2 mM NaF, 1 mM sodium orthovanadate, leupeptin (10 μg/ml), chymostatin (10 μg/ml), and pepstatin (10 μg/ml)], and crude cytoplasm was collected after centrifugation for 2 min in a Beckman E microcentrifuge with right angle rotor. Cytoplasm was promptly added to 0.2 volumes of 6X Laemmli sample buffer. Proteins were separated on 10.5% (100:1 acrylamide:bisacrylamide) polyacrylamide SDS gels and transferred to polyvinylidene difluoride membranes. p42 MAP kinase was detected with polyclonal antiserum DC3 [K.-M. Hsiao, S.-y. Chou, S.-J. Shih, J. E. Ferrell Jr., Proc. Natl. Acad. Sci. U.S.A. 91, 5480 (1994)].
23. 4, 5 mM Hepes (pH 7.8) [R. A. Wallace, D. W. Jared, J. N. Dumont, M. W. Sega, J. Exp Zool. 184, 321 (1973)]}. Oocytes were treated with progesterone or microinjected with purified recombinant malE-Mos, incubated for 8 to 10 hours, and then collected individually and frozen on dry ice. Individual oocytes were lysed by the addition of ice cold lysis buffer (50 to 100 μl) [100 mM NaCl, 50 mM β-glycerolphosphate (pH 7.4), 10 mM EDTA, 2 mM NaF, 1 mM sodium orthovanadate, leupeptin (10 μg/ml), chymostatin (10 μg/ml), and pepstatin (10 μg/ml)], and crude cytoplasm was collected after centrifugation for 2 min in a Beckman E microcentrifuge with right angle rotor. Cytoplasm was promptly added to 0.2 volumes of 6X Laemmli sample buffer. Proteins were separated on 10.5% (100:1 acrylamide:bisacrylamide) polyacrylamide SDS gels and transferred to polyvinylidene difluoride membranes. p42 MAP kinase was detected with polyclonal antiserum DC3 [K.-M. Hsiao, S.-y. Chou, S.-J. Shih, J. E. Ferrell Jr., Proc. Natl. Acad. Sci. U.S.A. 91, 5480 (1994)].
24. H for the experimentally determined oocyte distributions (Figs. 1 and 2).
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33. active][Mos] (where the square brackets indicate concentration), and so the steady-state concentration of Mos-P is (Formula Presented) Substituting Eq. 8 into Eq. 10 yields (Formula Presented) The roots of this equation are the possible steady-state concentrations of Mos-P. This equation was solved numerically with Mathematics 2.2.2 (Wolfram Research, Champaign, IL). Equations 8 and 9 were then used to calculate the corresponding concentrations of active and phosphorylated MAPK (Fig. 3B). Other things being equal, as the Hill coefficient increases, the concentration of malE-Mos needed for the switching between an off state and an on state becomes larger and the "completeness" of the switching becomes greater. A Hill coefficient of 3 for MAPK phosphorylation and of 5 for MAPK activation is sufficient to produce switching with a threshold and completeness that agree well with what is observed experimentally (Fig. 3B).
34. The response of MAPK phosphorylation to malE-Mos, as measured here, is expected to exhibit a Hill coefficient of at least half that seen for the response of MAPK activation to malE-Mos, measured previously (8).
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40. We thank M. Murakami and G. Vande Woude for providing malE-Mos plasmids and C.-Y. F. Huang for expressing and purifying malE-Mos. Supported by a grant from NIH (GM46383) and the Stanford University Cancer Biology Training Grant (CA09302).