Table 2.
Interactions between wild‐type coat protein (CP) and helper component‐proteinase (HC‐Pro) mutants.
| ASM (BD)* | Interaction with CP (AD)† | |
|---|---|---|
| Colony | α‐Gal | |
| HC‐Pro wt | ++ | Blue |
| HC‐Pro T310A | ++ | Blue |
| HC‐Pro H429A | ++ | Blue |
| HC‐Pro K432A | ++ | Blue |
| HC‐Pro D446A | ++ | Blue |
| HC‐Pro E450A | ++ | Blue |
| HC‐Pro K452A | ++ | Blue |
| HC‐Pro R455A | − | White |
AD, activation domain; ASM, alanine‐substituted mutant; BD, binding domain.
*
The amino acid substitution mutants of HC‐Pro were fused downstream of the GAL4 DNA‐binding domain (GAL4‐BD) of pAS2‐1.
†
Yeast cells co‐transformed with pACT2 and pAS2‐1 fusion derivatives were selected on synthetic dropout (SD) agar medium lacking leucine, tryptophan, histidine and adenine (–LWHA), and their α‐galactosidase activities were assayed on SD/–LW and SD/–LWHA agar plates containing X‐α‐Gal. The number of ‘+’ symbols indicates the comparative number of colonies formed on SD medium.