Oligomeric Assembly and Ligand Binding of the Members of Protein Family YER057c/YIL051c/YJGF

• Published in: Bioconjugate chemistry 2003-11, Vol.14 (6), p.1243-1252
• Main Authors: Mistiniene, Edita, Luksa, Virginijus, Sereikaite, Jolanta, Naktinis, Vytautas
• Format: Article
• Language: English
• Subjects: Anilino Naphthalenesulfonates - chemistry; Animals; Binding Sites; Chromatography, Liquid; Electrophoresis, Polyacrylamide Gel; Escherichia coli - genetics; Fatty Acids - metabolism; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - genetics; Humans; Kinetics; Ligands; Neoplasm Proteins - chemistry; Neoplasm Proteins - genetics; Protein Binding; Recombinant Fusion Proteins - chemistry; Spectrometry, Mass, Electrospray Ionization
• ISSN: 1043-1802; 1520-4812
• DOI: 10.1021/bc0341066

Proteins UK114 and p14.5 are both members of the putative family of small proteins YER057c/YIL051c/YjgF. The biological role of these proteins is not understood very well, and in addition, their oligomeric structure in solution remains controversial. We therefore investigated the oligomeric structure of UK114 and p14.5 using a number of methods. Both proteins have exhibited a homotrimeric structure in solution. Indeed the trimeric structure of the two proteins appeared to be so similar that when protein subunits derived from different species were mixed, stable heterotrimeric complexes (monomer ratio of 1:2 and 2:1 of UK114 and p14.5, respectively) could be formed in vitro. Furthermore, the trimeric structure of both UK114 and p14.5 proved essential for the stoichiometric hydrophobic ligand, such as fatty acid binding activity of the two proteins.