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The sequence of the β-hydroxy-β-methylglutaryl coenzyme A reductase (HMGR) promoter contains two E26S-box motifs and a CYP7A1 promoter element. In order to investigate whether these motifs are responsible for post-translational ubiquitination of exogenous HMGR and targeted by polyubiquitin chains for degradation by the 26S proteasome, we constructed a pYZP-HMGR plasmid in which the FMGR signal peptide was fused to the N-terminus of the HMGR cDNA. N-terminal sequence analyses revealed a modification of the C-terminal Met residue by a Gly residue. This modification was not detectable when the recombinant HMGR protein (rHMGR) was expressed in Escherichia coli and purified in a urea-containing buffer. Post-translational degradation of rHMGR by the 26S proteasome was also observed in E. coli. The effects of an N-terminal sequence mutation on post-translational ubiquitination and degradation of exogenous rHMGR by the 26S proteasome in Hep G2 cells were then examined. A C-terminal Met-to-Thr mutation of rHMGR increased the half-life of the protein from 10 to 22 h. The addition of a Thr residue at the N-terminal of the rHMGR protein blocked its degradation by the 26S prote
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