Table 1.
Interactions between coat protein (CP) mutants and wild‐type (wt) helper component‐proteinase (HC‐Pro).
| ASM (AD)* | Interaction with HC‐Pro (BD)† | |
|---|---|---|
| Colony | α‐Gal | |
| CP wt | ++ | Blue |
| CP G12E | − | White |
| CP D133A | ++ | Blue |
| CP E135A | ++ | Blue |
| CP E136A | ++ | Blue |
| CP E139A | ++ | Blue |
| CP K143A | ++ | Blue |
| CP E147A | ++ | Blue |
| CP D133A+E135A | ++ | Blue |
| CP D133A+E136A | ++ | Blue |
| CP E135A+E136A | ++ | Blue |
| CP H246A | ++ | Blue |
| CP R249A | ++ | Blue |
| CP D250A | ++ | Blue |
| CP H256A | − | White |
AD, activation domain; ASM, alanine‐substituted mutant; BD, binding domain.
*
The amino acid substitution mutants of CP were fused downstream of the GAL4 activation domain (GAL4‐AD) of pACT2.
†
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.