TY - JOUR
T1 - Biotin induces tetramerization of a recombinant monomeric avidin. A model for protein-protein interactions
AU - Laitinen, Olli H.
AU - Marttila, Ari T.
AU - Airenne, Kari J.
AU - Kulik, Tikva
AU - Livnah, Oded
AU - Bayer, Edward A.
AU - Wilchek, Meir
AU - Kulomaa, Markku S.
PY - 2001/3/16
Y1 - 2001/3/16
N2 - Chicken avidin, a homotetramer that binds four molecules of biotin was converted to a monomeric form by successive mutations of interface residues to alanine. The major contribution to monomer formation was the mutation of two aspartic acid residues, which together account for ten hydrogen bonding interactions at the 1-4 interface. Mutation of these residues, together with the three hydrophobic residues at the 1-3 interface, led to stable monomer formation in the absence of biotin. Upon addition of biotin, the monomeric avidin reassociated to the tetramer, which exhibited properties similar to those of native avidin, with respect to biotin binding, thermostability, and protease resistance. To our knowledge, these unexpected results represent the first example of a small monovalent ligand that induces oligomerization of a monomeric protein. This study may suggest a biological role for low molecular weight ligands in inducing oligomerization and in maintaining the stability of multimeric protein assemblies.
AB - Chicken avidin, a homotetramer that binds four molecules of biotin was converted to a monomeric form by successive mutations of interface residues to alanine. The major contribution to monomer formation was the mutation of two aspartic acid residues, which together account for ten hydrogen bonding interactions at the 1-4 interface. Mutation of these residues, together with the three hydrophobic residues at the 1-3 interface, led to stable monomer formation in the absence of biotin. Upon addition of biotin, the monomeric avidin reassociated to the tetramer, which exhibited properties similar to those of native avidin, with respect to biotin binding, thermostability, and protease resistance. To our knowledge, these unexpected results represent the first example of a small monovalent ligand that induces oligomerization of a monomeric protein. This study may suggest a biological role for low molecular weight ligands in inducing oligomerization and in maintaining the stability of multimeric protein assemblies.
UR - http://www.scopus.com/inward/record.url?scp=0035896602&partnerID=8YFLogxK
U2 - 10.1074/jbc.M007930200
DO - 10.1074/jbc.M007930200
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C2 - 11076945
AN - SCOPUS:0035896602
SN - 0021-9258
VL - 276
SP - 8219
EP - 8224
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 11
ER -