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. 2002 Nov 15;21(22):6061–6071. doi: 10.1093/emboj/cdf626

graphic file with name cdf626f7.jpg

Fig. 7. Degradation of either Xenopus or mouse MOS in mouse NIH 3T3 cells, Xenopus XTC cells and rabbit reticulocyte lysate does not depend on the N-terminal Pro residue of MOS. Positions of fDHFR-UbR48 and either Xenopus MOS (MOS) or mouse MOS (mMOS) are indicated on the left. (A) Pulse–chase in mouse NIH 3T3 cells. Lanes a–d, Pro-Ser-mMOS; lanes e–h, Gly-Ser-mMOSP2G; lanes i–l, Arg-Ser-mMOSP2R. (B) Mutations at Ser-2 (encoded Ser-3) have a negligible effect on degradation of mouse MOS in NIH 3T3 cells. Lanes a–d, Pro-Ser-mMOS; lanes e–h, Pro-Ala-mMOSS3A; lanes i–l, Pro-Glu-mMOSS3E. (CXenopus MOS is long-lived in Xenopus XTC cells. Lanes a–c, Pro-Ser-MOS; lanes d–f, Gly-Ser-MOSP2G. (D) N-terminal Pro of Xenopus MOS does not metabolically destabilize MOS in rabbit reticulocyte lysate. Lanes a–d, Pro-Ser-MOS; lanes e–h, Gly-Ser-MOSP2G.