Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis
Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis
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DOI:
10.1016/j.febslet.2011.01.005
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发表时间:
2011-02-04
期刊:
影响因子:
3.5
通讯作者:
Marahiel, Mohamed A.
中科院分区:
文献类型:
--
作者:
Albrecht, Alexander G.;Peuckert, Florian;Marahiel, Mohamed A.
Iron-sulfur cluster biosynthesis in Gram-positive bacteria is mediated by the SUF system. The transfer of sulfide from the cysteine desulfurase SufS to the scaffold protein SufU is one of the first steps within the assembly process. In this study, we analyzed the interaction between Bacillus subtilis SufS and its scaffold SufU. The activity of SufS represents a Ping-Pong mechanism leading to successive sulfur loading of the conserved cysteine residues in SufU. Cysteine 41 of SufU is shown to be essential for receiving sulfide from SufS, while cysteines 66 and 128 are needed for SufS/SufU interaction. In conclusion, we present the first step-by-step model for loading of the essential scaffold component SufU by its sulfur donor SufS.Structured summary:SufS and SufU bind by molecular sieving (View interaction)SufS binds to SufS by molecular sieving (View interaction)SufS and SufU redox react by enzymatic study (View Interaction 1, 2, 3, 4, 5)SufU physically interacts with SufS by pull down (View Interaction 1, 2) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.