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J. Biol. Chem., Vol. 264, Issue 13, 7267-7275, 05, 1989
SC Chen, G Kramer and B Hardesty
A Mr 60,000 peptide that modulates the activity of the Mr 35,000 catalytic
subunit of a type 2A phosphatase has been isolated from rabbit
reticulocytes and partially characterized. The peptide appears to be a
subunit of the intact phosphatase that has been isolated under
nondenaturing conditions. The Mr 60,000 peptide itself is catalytically
inactive. However, it binds to the Mr 35,000 catalytic subunit causing a
decrease in its activity for dephosphorylation of phosphorylated 40 S
ribosomal subunits, but an increase in dephosphorylation of peptide
initiation factor 2 phosphorylated in its alpha subunit. Reassociation of
the Mr 60,000 and the Mr 35,000 peptides yields a two-subunit phosphatase
with a Stokes radius of 42 A; sedimentation coefficient, S20,w of 5.1 S;
molecular weight of 89,000. These parameters are compared to those of the
native three-subunit enzyme and those of the isolated Mr 35,000 and 60,000
peptides.
Isolation and partial characterization of an Mr 60,000 subunit of a type 2A phosphatase from rabbit reticulocytes
Clayton Foundation Biochemical Institute, Department of Chemistry, University of Texas, Austin 78712.
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