Three protein kinase C (PKC)-eta mutants were constructed in which the
whole or part of the pseudosubstrate site was replaced with correspon
ding parts of the PKC-alpha pseudosubstrate site. The resulting chimae
ric kinases were compared with wild-type PKC-eta in their ability to p
hosphorylate a PKC-eta peptide substrate or histone. Changes in the ps
eudosubstrate site of PKC-eta are accompanied by changes in substrate
selectivity, indicating that the substrate selectivity observed for PK
C-eta is at least in part due to its pseudosubstrate site.