), we have determined that the KIN28 gene used in two of our experiments ( Fig. 3 and 6) contains two additional mutations that arose during PCR amplification of the sequence from a cDNA library. These mutations result in two amino acid changes in nonconserved regions of the Kin28 protein kinase sequence (N123D and M273T). Since this double mutant gene allows growth of kin28-3 cells and encodes a Kin28 protein with abundant kinase activity ( Fig. 3 and 6), these two mutations do not abolish Kin28 function. However, the presence of these mutations does appear to have an impact on the requirement for T162 phosphorylation in Kin28 function. We showed in Fig. 3 that the T162A mutation blocks Kin28 function, suggesting that phosphorylation at this site might be required for full function. However, G. Faye (unpublished data) and M. Solomon's group (J. Kimmelman, P. Kaldis, C.
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