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J. Biol. Chem., Vol. 269, Issue 22, 15563-15570, 06, 1994
S Huff, YV Matsuka, MJ McGavin and KC Ingham
The N-terminal 29-kDa fragment of fibronectin (Fn29K) contains five type I
"finger" modules. It binds to heparin, fibrin, and bacteria and is involved
in fibronectin (Fn) matrix assembly. Binding to Staphylococcus aureus
involves a cell wall-associated protein that contains approximately three
repeats of a 38-residue D motif (Signas, C., Raucci, G., Jonsson, K.,
Lindgren, P.-E., Anantharamaiah, G.M., Hook, M., and Lindberg, M. (1989)
Proc. Natl. Acad. Sci. U.S.A. 86, 699- 703). Synthetic peptides
representing D1, D2, and D3, when labeled with fluorescein isothiocyanate
(FITC), exhibited increases in fluorescence anisotropy upon addition of
Fn29K but not other Fn fragments. The response could be reversed by
titration with unlabeled peptides to yield inhibition constants that agreed
with the dissociation constants obtained by fitting the initial response.
Values of Kd ranged between 2 and 12 microM, with D3 having the highest
affinity. Specificity of D3 for Fn29K was further illustrated by the fact
that its C-terminal half (D3b, Lys801 to Lys821), when immobilized,
selectively adsorbed Fn29K from a thermolysin digest of fibronectin. The
binding site in Fn was further localized within Fn29K by analyzing smaller
proteolytic or recombinant subfragments. Those containing fingers, F3-5 and
F4-5, were purified on D3b-Sepharose and bound FITC-D3b with Kd values of
4-6 microM. Subfragments containing pairs of fingers 1-2, 2-3, or single
fingers 1, 4, or 5 were inactive. Whole D1-3, expressed in Escherichia coli
and labeled with fluorescein, bound 1.9 mol/mol of Fn29K with Kd = 1.5 nM.
F4-5 and F2-3 bound with respective Kd values of 0.35 and 4.4 microM. These
and other results indicate that binding of the individual D region peptides
is mediated through their C-terminal halves, primarily to fingers 4 and 5
of fibronectin. The possible basis of the much higher affinity of D1-3 is
discussed.
Interaction of N-terminal fragments of fibronectin with synthetic and recombinant D motifs from its binding protein on Staphylococcus aureus studied using fluorescence anisotropy
Holland Laboratory, American Red Cross, Rockville, Maryland 20855.
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