Hsp90 is a molecular chaperone essential to the folding, activation and maturation of small number of distinct client proteins. We hypothesize that PKCα is a possible client protein of Hsp90; we base this hypothesis according to the results from Rotenberg laboratory showing that Hsp90 and PKCα co-immunoprecipitate. A sub-cloning project was done as part of this bigger project. We subcloned bovine PKCα-3HA gene into a yeast plasmid. In order to accomplish my project, I digested a mammalian plasmid pCMV4 PKCα with EcoRI & XhoI restriction enzymes. Then I cleaned the DNA fragments from a gel. This was followed by a Ligation reaction with Vector and Insert fragments. The recombinant DNA was transformed with E.coli DH5α competent cells. We selected on the LB & Amp plates. Finally we confirmed our recombinant plasmid that has bovine PKCα-3HA gene in the new yeast plasmid by a) EcoRI & XhoI digestion and running gel b) PCR amplification of PKCα gene-3HA in the new plasmid and finally c) sequencing the gene. This gene will be expressed in different yeast strains and the amount of protein and its activity will be measured.