The identification and characterisation of an actin‐binding site in α‐actinin by mutagenesis

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Abstract
We have shown previously that the N‐terminal actin‐binding domain of α‐actinin retains activity when expressed in E. coli as a fusion protein with glutathione‐S‐transferase. In the present study we have made a series of N‐ and C‐terminal deletions within this domain and show that an actin‐binding site is contained within residues 120–134. Amino acid substitutions within this region indicate that several highly conserved hydrophobic residues are involved in binding to F‐actin. The hypothesis that the interaction between α‐actinin and F‐actin is predominantly hydrophobic in nature is supported by the observation that binding is relatively independent of salt concentration.