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Phosphorylation of SV40 large T antigen at threonine residues results in conversion to a lower apparent molecular weight form (1992)

Grässer, F. A. ; König, S.

Springer

Archives of virology 126 (1992), S. 313-320

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ISSN: 1432-8798

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Summary Simian virus 40 large T antigen (large T) was dephosphorylated with potato acid phosphatase at pH 5.5. Phosphate residues bound to serine were more susceptible to potato acid phosphatase than threonine-bound phosphate residues. Dephosphorylation of the threonine residues with potato acid phosphatase resulted in a reduced gelelectrophoretic mobility, while removal of the remaining phosphate groups had no effect on the mobility of large T. Pulsechase experiments revealed a slower migrating form of newly synthesized large T which was converted by phosphorylation to a faster migrating form and had a half-life of approximately 1 h.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF01309704

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