The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA
The Biosynthesis of the Molybdenum Cofactor in Escherichia coli and Its Connection to FeS Cluster Assembly and the Thiolation of tRNA
复制标题
大肠杆菌中钼辅因子的生物合成及其与 FeS 簇组装和 tRNA 硫醇化的关系
DOI:
10.1155/2014/808569
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发表时间:
2015
期刊:
影响因子:
--
通讯作者:
Leimkühler S
中科院分区:
文献类型:
--
作者:
Mendel RR;Leimkühler S
The thiolation of biomolecules is a complex process that involves the activation of sulfur. The L‐cysteine desulfurase IscS is the main sulfur mobilizing protein inEscherichia colithat provides the sulfur from L‐cysteine to several important biomolecules in the cell such as iron sulfur (FeS) clusters, molybdopterin (MPT), thiamine, and thionucleosides of tRNA. Various proteins mediate the transfer of sulfur from IscS to various biomolecules using different interaction partners. A direct connection between the sulfur‐containing molecules FeS clusters, thiolated tRNA, and the molybdenum cofactor (Moco) has been identified. The first step of Moco biosynthesis involves the conversion of 5′GTP to cyclic pyranopterin monophosphate (cPMP), a reaction catalyzed by a FeS cluster containing protein. Formed cPMP is further converted to MPT by insertion of two sulfur atoms. The sulfur for this reaction is provided by the L‐cysteine desulfurase IscS in addition to the involvement of the TusA protein. TusA is also involved in the sulfur transfer for the thiolation of tRNA. This review will describe the biosynthesis of Moco inE. coliin detail and dissects the sulfur transfer pathways for Moco and tRNA and their connection to FeS cluster biosynthesis.
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影响因子:
3.5
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DOI:
--
发表时间:
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期刊:
The Journal of biological chemistry
影响因子:
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作者:
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通讯作者:
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