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J. Biol. Chem., Vol. 269, Issue 45, 27863-27868, Nov, 1994
KM Aguirre, RJ McCormick and JE Schwarzbauer
The formation of a fibrillar fibronectin (FN) extracellular matrix requires
self-association of FN dimers. In this report, we show that the major sites
for self-association are the amino-terminal repeats I1- 5 and the first
type III repeats. Recombinant FNs and fragments were generated by
baculovirus expression of cysteine-rich domains and by bacterial expression
of type III repeats as fusion proteins with maltose binding protein. When
recombinant polypeptides were immobilized on microtiter wells, FN bound to
70-kDa amino-terminal fragment and to fusion proteins containing repeats
III1-2 and III1-6 but not to other type III repeats. Similar results were
obtained with a gel overlay assay. Binding was concentration-dependent and
saturable. The amino- terminal binding site for III1-2 was further
localized to repeats I1-5. Therefore, at least two different sites for
FN-FN interaction reside near the amino terminus of the molecule. A model
for the regulation of FN matrix assembly is proposed based on
intramolecular interactions between these amino-terminal sites.
Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule
Department of Molecular Biology, Princeton University, New Jersey 08544- 1014.
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