The Mammalian Proteins MMS19, MIP18, and ANT2 Are Involved in Cytoplasmic Iron-Sulfur Cluster Protein Assembly

Niek van Wietmarschen, Annie Moradian, Gregg B. Morin, Peter M. Lansdorp, Evert-Jan Uringa*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

37 Citations (Scopus)

Abstract

Iron-sulfur (Fe-S) clusters are essential cofactors of proteins with a wide range of biological functions. A dedicated cytosolic Fe-S cluster assembly (CIA) system is required to assemble Fe-S clusters into cytosolic and nuclear proteins. Here, we show that the mammalian nucleotide excision repair protein homolog MMS19 can simultaneously bind probable cytosolic iron-sulfur protein assembly protein CIAO1 and Fe-S proteins, confirming that MMS19 is a central protein of the CIA machinery that brings Fe-S cluster donor proteins and the receiving apoproteins into proximity. In addition, we show that mitotic spindle-associated MMXD complex subunit MIP18 also interacts with both CIAO1 and Fe-S proteins. Specifically, it binds the Fe-S cluster coordinating regions in Fe-S proteins. Furthermore, we show that ADP/ATP translocase 2 (ANT2) interacts with Fe-S apoproteins and MMS19 in the CIA complex but not with the individual proteins. Together, these results elucidate the composition and interactions within the late CIA complex.

Original languageEnglish
Pages (from-to)43351-43358
Number of pages8
JournalThe Journal of Biological Chemistry
Volume287
Issue number52
DOIs
Publication statusPublished - 21-Dec-2012

Keywords

  • SACCHAROMYCES-CEREVISIAE
  • DNA-REPLICATION
  • TRANSCRIPTION
  • BIOGENESIS
  • REPAIR
  • IDENTIFICATION
  • METABOLISM
  • MATURATION
  • COMPONENT
  • COMPLEX

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