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

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 structur...

Full description

Saved in:
Bibliographic Details
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
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:1043-1802
1520-4812
DOI:10.1021/bc0341066