The phage lambda repressor activates transcription of its own gene from the promoter PRM. Previous work has suggested that this activation involves a protein-protein interaction between DNA-bound repressor and RNA polymerase. To identify the subunit of RNA polymerase that participates in this putative interaction, we searched for polymerase mutants that responded poorly to repressor. We report here the isolation of three sigma mutants that caused defects in repressor-stimulated, but not basal, transcription from PRM. These mutants bear amino acid substitutions in a putative helix-turn-helix motif that sigma uses to recognize the promoter -35 region. We suggest that lambda repressor interacts directly with this helix-turn-helix motif in facilitating the formation of a productive initiating complex.