Localization of a new alpha-actinin binding site in the COOH-terminal part of actin sequence.
The interaction of filamentous actin with alpha-actinin, an actin cross-linking protein, is well established. On the other hand, monomeric actin-alpha-actinin interaction has been a subject of controversy. In this report, we have characterized the interaction of monomeric actin, coated on plastic plates under conditions of non-polymerization, with alpha-actinin in presence of magnesium. Using specific polyclonal anti-actin antibodies, with the whole molecule or purified peptides, we have localized two sites of interaction on action molecule: one near Thr-103 and a new one in the twenty last amino acids.
Lebart
M C
MC
Centre de Recherches de Biochimie Macromoléculaire (CNRS), U. 249 (INSERM), Université de Montpellier I, France.
Méjean
C
C
Boyer
M
M
Roustan
C
C
Benyamin
Y
Y
D000185:Actinin / Q000302:isolation & purification / Q000378:metabolism*; D000199:Actins / Q000378:metabolism*; D000818:Animals; D001665:Binding Sites; D002645:Chickens; D004797:Enzyme-Linked Immunosorbent Assay; D005895:Gizzard, Avian / Q000378:metabolism; D007106:Immune Sera; D007700:Kinetics; D009130:Muscle, Smooth / Q000378:metabolism; D013912:Threonine
D000199:Actins; D007106:Immune Sera; D000185:Actinin; D013912:Threonine