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The starch synthase 4 (SS4) is a key enzyme for initiation of starch granules and regulation of the starch granule number in chloroplasts of higher plants. These enzymes transfer glucosyl residue from ADPglucose to the non-reducing end of a preexisting glucan chain. The presence of a coiled-coil motive in the N-terminus of Arabidopsis SS4 has been involved in mediating some of the protein-protein interactions. Thus, it was also shown that AtSS4 directly interacts with the plastidial phosphorylase (AtPHS1). However, phosphorylase enzymes are widespread in animals, microorganism, and plants. So far, it was unclear if the observed protein-protein interaction is specific for plant origin phosphorylase enzymes. Therefore, we tested whether or not an animal type phosphorylase, the rabbit muscle phosphorylase a (Pho a), also interacts with AtSS4. Our results show that the protein-protein interaction of AtPHS1 and AtSS4 is specific and cannot archived by Pho a. Furthermore, also a functional interaction between AtSS4 and the Pho a was not detected.

scholars international journal of biochemistry

Identify the Specificity of Interaction between the Arabidopsis Starch Synthase 4 and the Plastidial Starch Phosphorylase using a Homologous Protein-Animal Rabbit Muscle Phosphorylase a