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Characterization of serine kinase activity associated with Moloney murine sarcoma virus V-mos gene products

Thesis/Dissertation ·
OSTI ID:6106736
Various Moloney murine sarcoma virus (Mo-MuSV) isolates contain a cellular sequence, termed mos, which is responsible for the transforming ability of Mo-MuSV. A serine kinase activity has been found to be associated with mos gene product of several isolates of Mo-MuSV. A mutants of Mo-MuSV strain 124 (designated MuSV ts 110) is temperature-sensitive (ts) for transformation and encodes two proteins, P85/sup gag-mos/ and P58/sup gag/, at the permissive temperature (28/sup 0/C). At the nonpermissive temperature (39/sup 0/C), only P58/sup gag/ is found in MuSV ts 110-infected NRK cells (6m2 cells). Both P85/sup gag-mos/ and P58/sup gag/ were phosphorylated when anti-gag immune complexes containing these proteins were incubated at 22/sup 0/C with (lambda-/sup 32/P)-ATP and MnCl/sub 2/. The kinase detected in anti-gag complexes from 6m2 cells at permissive temperature was associated with P85/sup gag-mos/ since immune complexes from 39/sup 0/C 6m2 cells, which lack P85/sup gag-mos/, produced no phosphorylated P58/sup gag/ molecules. Using the optimal conditions developed for the P85/sup gag-mos/ kinase, Mo-MuSV-encoded p37/sup mos/ was also found to be associated with a serine kinase activity. Antibodies directed against the C-terminus of v-mos were found to inhibit the in vitro phosphorylation of p37/sup mos/, suggesting that the extreme C-terminal sequence of v-mos may be important for an intrinsic kinase activity. This inhibitory action by antibodies to the C-terminus of p37/sup mos/, when considered with all the other data reported here, provides convincing evidence that the v-mos gene encodes a serine protein kinase activity.
Research Organization:
Texas Univ., Houston (USA). Graduate School of Biomedical Sciences
OSTI ID:
6106736
Country of Publication:
United States
Language:
English