Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility.
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Fibronectin (FN) is an extracellular matrix protein that is assembled into fibrils by cells during tissue morphogenesis and wound healing. FN matrix fibrils are highly elastic, but the mechanism of elasticity has been debated: it may be achieved by mechanical unfolding of FN-III domains or by a conformational change of the molecule without domain unfolding. Here, we investigate the folded state of FN-III domains in FN fibrils by measuring the accessibility of buried cysteines. Four of the 15 FN-III domains (III-2, -3, -9, and -11) appear to unfold in both stretched fibrils and in solution, suggesting that these domains spontaneously open and close even in the absence of tension. Two FN-III domains (III-6 and -12) appear to unfold only in fibrils and not in solution. These results suggest that domain unfolding can at best contribute partially to the 4-fold extensibility of fibronectin fibrils.
SubjectNIH 3T3 Cells
Protein Structure, Tertiary
Published Version (Please cite this version)10.1074/jbc.m111.240028
Publication InfoErickson, Harold Paul; Lemmon, Christopher A; & Ohashi, Tomoo (2011). Probing the folded state of fibronectin type III domains in stretched fibrils by measuring buried cysteine accessibility. The Journal of biological chemistry, 286(30). 10.1074/jbc.m111.240028. Retrieved from https://hdl.handle.net/10161/16458.
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James B. Duke Professor of Cell Biology
Cytoskeleton: It is now clear that the actin and microtubule cytoskeleton originated in bacteria. Our major research is on FtsZ, the bacterial tubulin homolog, which assembles into a contractile ring that divides the bacterium. We have studied FtsZ assembly in vitro, and found that it assembles into thin protofilaments (pfs). Dozens of these pfs are further clustered to form the contractile Z-ring in vivo. Some important discoveries in the last ten years include: &bul
Assistant Research Professor of Cell Biology
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