MMS19 links cytoplasmic iron-sulfur cluster assembly to DNA metabolism.
The function of many DNA metabolism proteins depends on their ability to coordinate an iron-sulfur (Fe-S) cluster. Biogenesis of Fe-S proteins is a multistep process that takes place in mitochondria and the cytoplasm, but how it is linked to nuclear Fe-S proteins is not known. Here, we demonstrate that MMS19 ... forms a complex with the cytoplasmic Fe-S assembly (CIA) proteins CIAO1, IOP1, and MIP18. Cytoplasmic MMS19 also binds to multiple nuclear Fe-S proteins involved in DNA metabolism. In the absence of MMS19, a failure to transfer Fe-S clusters to target proteins is associated with Fe-S protein instability and preimplantation death of mice in which Mms19 has been knocked out. We propose that MMS19 functions as a platform to facilitate Fe-S cluster transfer to proteins critical for DNA replication and repair.
Mesh Terms:
Amino Acid Sequence, Animals, Carrier Proteins, Cytoplasm, DNA, DNA Repair, DNA Replication, Humans, Hydrogenase, Iron-Sulfur Proteins, Metallochaperones, Mice, Mice, Knockout, Molecular Sequence Data, Nuclear Proteins, Protein Stability, Saccharomyces cerevisiae, Transcription Factors, Xeroderma Pigmentosum Group D Protein
Amino Acid Sequence, Animals, Carrier Proteins, Cytoplasm, DNA, DNA Repair, DNA Replication, Humans, Hydrogenase, Iron-Sulfur Proteins, Metallochaperones, Mice, Mice, Knockout, Molecular Sequence Data, Nuclear Proteins, Protein Stability, Saccharomyces cerevisiae, Transcription Factors, Xeroderma Pigmentosum Group D Protein
Science
Date: Jul. 13, 2012
PubMed ID: 22678361
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