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2015 | 2 | 1 |
Tytuł artykułu

Stabilization of the “open” conformer of apoIscU on the surface of polystyrene nanobeads accelerates assembly of a 2Fe2S structure

Treść / Zawartość
Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The scaffold protein IscU is involved in the assembly/transfer of FeS clusters. IscU exists in both open and closed conformation. The clusterless open conformation of IscU adheres to the hydrophobic surface of polystyrene nanobeads, as observed for other proteins. Increased accessibility of the ligand cysteines in bound IscU facilitates assembly of a 2Fe2S cluster, and the cluster-bearing structured form of IscU does not interact with the nanobeads, thus ensuring turnover. The dependence of accelerated cluster assembly on the nanobeads concentration pointed to steric and crowding effects as for promoting cluster formation, and confirms the requirement for structural flexibility of IscU .
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Wydawca

Czasopismo
Rocznik
Tom
2
Numer
1
Opis fizyczny
Daty
otrzymano
2015-07-13
zaakceptowano
2015-09-27
online
2016-01-20
Twórcy
  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan
  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan
  • DeFENS, University of
    Milan, Via Celoria 2, 20133, Milan, Italy
  • Section of
    Chemical and Biomolecular Sciences, DeFENS, University of Milan
Bibliografia
  • [1] Ciesielski S.J., Schilke B.A., Osipiuk J., Bigelow L., Mulligan R.,Majewska J., Joachimiak A., Marszalek J., Craig E.A., DutkiewiczR., Interaction of J-protein co-chaperone Jac1 with Fe-S scaffoldIsu is indispensable in vivo and conserved in evolution, J. Mol.Biol., 2012, 417, 1-12.[WoS]
  • [2] Johnson D.C., Dean D.R., Smith A.D., Johnson M.K., Structure,function and formation of biological iron-sulfur clusters, Annu.Rev. Biochem., 2005, 78, 247–281.
  • [3] Rouault T.A., Tong W.H., Iron–sulphur cluster biogenesis andmitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol., 2005,6, 345–351.
  • [4] Ayala-Castro C., Saini A., Outten F.W., Fe–S cluster assemblypathways in bacteria, Microbiol. Mol. Biol. Rev., 2008, 72,110–125.
  • [5] Raulfs E.C., O’Carroll I.P., Dos Santos P.C., Unciuleac M.-C.,Dean D.R., In vivo iron sulfur cluster formation, Proc. Natl.Acad. Sci. U.S.A., 2008, 105, 8591-8596.
  • [6] Chandramouli K., Unciuleac M.C., Naik S., Dean D.R., HuynhB.H., Johnson M.K., Formation and properties of [4Fe-4S]clusters on the IscU scaffold protein. Biochemistry, 2007, 46,6804-6811.[WoS]
  • [7] Unciuleac M.C., Chandramouli K., Naik S., Mayer S.,Huynh B.H., Johnson M.K., Dean D.R., In vitro activation ofapo-aconitase using a [4Fe-4S] cluster-loaded form of the IscU[WoS]
  • [Fe-S] cluster scaffolding protein. Biochemistry, 2007, 46,6812-6821.
  • [8] Shakamuri P., Zhang B., Johnson M.K., Monothiol glutaredoxinsfunction in storing and transporting [Fe2S2] clustersassembled on IscU scaffold proteins, J. Am. Chem. Soc., 2012,134, 15213-15216.[WoS]
  • [9] Bonomi F., Iametti S., Morleo A., Ta D.T., Vickery L.E., Studieson the mechanism of catalysis of iron-sulfur cluster transferfrom IscU
  • [2Fe2S] by HscA/HscB chaperones, Biochemistry,2011, 50, 9641-9650.
  • [10] Bonomi F., Iametti S., Morleo A., Ta D.T., Vickery L.E., Facilitatedtransfer of IscU-[2Fe2S] clusters by chaperone-mediated ligandexchange, Biochemistry, 2008, 47, 12795-12801.[WoS]
  • [11] Bonomi F., Iametti S., Ta D.T., Vickery L.E., Multiple turnovertransfer of [2Fe2S] clusters by the iron-sulfur cluster assemblyscaffold proteins IscU and IscA, J. Biol. Chem., 2005, 280,29513-29518.
  • [12] Markley J.L., Kim J.H., Dai Z.Q., Bothe J.R., Cai K., FrederickR.O., Tonelli M., Metamorphic protein IscU alternates conformationsin the course of its role as the scaffold protein foriron-sulfur cluster biosynthesis and delivery, FEBS Letters,2013, 587, 1172-1179.[WoS]
  • [13] Yan R., Kelly G., Pastore A., The scaffold protein IscU retains astructured conformation in the Fe-S cluster assembly complex,Chem. Biochem., 2014, 15, 1682-1686.
  • [14] Miriani M., Eberini I., Iametti S., Ferranti P., Sensi C., Bonomi F.,Unfolding of beta-lactoglobulin on the surface of polystyrenenanoparticles: Experimental and computational approaches,Proteins 2014, 82, 1272–1282.
  • [15] Miriani M., Iametti S., Kurtz D.M., Bonomi F., Rubredoxinrefolding on nanostructured hydrophobic surfaces: Evidencefor a new type of biomimetic chaperones, Proteins 2014, 82,3154-3162.
  • [16] Kim J.H., Bothe J.R., Alderson T.R., Markley J.L., Tangled webof interactions among proteins involved in iron-sulfur clusterassembly as unraveled by NMR, SAXS, chemical crosslinking,and functional studies, Biochim. Biophys. Acta, 2015, 1853,1416-1428.[WoS]
  • [17] Maio N., Rouault T.A., Iron–sulfur cluster biogenesis inmammalian cells: New insights into the molecular mechanismsof cluster delivery, Biochim. Biophys. Acta, 2015, 1853,1493-1512.[WoS]
  • [18] Hoff K.G., Silberg J.J., Vickery L.E., Interaction of the iron-sulfurcluster assembly protein IscU with the Hsc66/Hsc20 molecularchaperone system of Escherichia coli, Proc. Natl. Acad. Sci.U.S.A., 2000, 97, 7790-7795.
  • [19] Morleo A., Bonomi F., Iametti S., Huang V.W., Kurtz D.M.,Iron-nucleated folding of a metalloprotein in high urea:resolution of metal binding and protein folding events,Biochemistry, 2010, 49, 6627–6634.[WoS]
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
bwmeta1.element.-psjd-doi-10_1515_ped-2015-0006
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