Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity.

S. P., Wu; Mansy, Sheref Samir; Cowan, J. A.

doi:10.1021/bi0483007

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IscU functions as a scaffold for Fe-S cluster assembly and transfer, and is known to be a substrate protein for molecular chaperones. Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Binding of DnaK reduces the rate of formation of the IscU−Fd complex (greater than 8-fold), but has little influence on the intrinsic rate of iron−sulfur cluster transfer to apo Fd. Apparently the molecular chaperone DnaK does not facilitate the process of Fe-S cluster transfer from IscU. Rather, DnaK has a modest influence on the stability of the IscU-bound Fe-S cluster that may reflect a more important role in promoting cluster assembly. In accord with prior observations the cochaperone DnaJ stimulates the ATPase activity of DnaK, but has a minimal influence on IscU cluster transfer activity, either alone or in concert with DnaK.

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Titolo:	Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity.
Autori Unitn:	S. P. Wu Mansy, Sheref Samir J. A. Cowan mostra contributor esterni nascondi contributor esterni
Anno di pubblicazione:	2005
Titolo del periodico:	BIOCHEMISTRY
Citazione:	Iron-sulfur cluster biosynthesis. Molecular chaperone DnaK promotes IscU-bound [2Fe-2S] cluster stability and inhibits cluster transfer activity. / S. P., Wu; Mansy, Sheref Samir; J. A., Cowan. - In: BIOCHEMISTRY. - ISSN 0006-2960. - STAMPA. - 44:11(2005), pp. 4284-4293.
Abstract:	IscU functions as a scaffold for Fe-S cluster assembly and transfer, and is known to be a substrate protein for molecular chaperones. Kinetic studies of Fe-S cluster transfer from holo IscU to apo Fd in the presence of chaperone DnaK demonstrate an inhibitory effect on the rate of Fe-S cluster transfer from IscU. Binding of DnaK reduces the rate of formation of the IscU−Fd complex (greater than 8-fold), but has little influence on the intrinsic rate of iron−sulfur cluster transfer to apo Fd. Apparently the molecular chaperone DnaK does not facilitate the process of Fe-S cluster transfer from IscU. Rather, DnaK has a modest influence on the stability of the IscU-bound Fe-S cluster that may reflect a more important role in promoting cluster assembly. In accord with prior observations the cochaperone DnaJ stimulates the ATPase activity of DnaK, but has a minimal influence on IscU cluster transfer activity, either alone or in concert with DnaK.
Handle:	http://hdl.handle.net/11572/89668
Appare nelle tipologie:	03.1 Articolo su rivista (Journal article)

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