Cloning and sequence analysis of a cDNA encoding bovine ribosomal protein P2: predicted alpha-helices and potential phosphorylation sites.

Abstract

A cDNA corresponding to bovine acidic ribosomal P2 was cloned and sequenced. It encodes a polypeptide 115 amino acids long. The secondary structure prediction shows that bovine P2 contains a large part of the protein domain as alpha helices. Alignment and analysis of 16 eukaryotic P2 proteins of 12 species reveal that there are three predicted alpha-helical regions conserved in almost all P2 proteins; helix 1 and helix 2 may be part of a helix-turn-helix structure. Sequence analysis indicates that there are seven serine residues in bovine P2 protein which are potential phosphorylation sites for a variety of Ser/Thr kinases. A few such sites appear at similar positions in many P2 proteins. The antigenic region is predicted to be located in the stretch of acidic amino acids in the vicinity of the C-terminus of P2. The predicted alpha-helical structures, potential phosphorylation sites and antigenic regions of the P2 protein provide some insights into the structure of P2 protein and deserve further experimental study.