The Nbp35/ApbC homolog acts as a nonessential [4Fe-4S] transfer protein in methanogenic archaea

FEBS Lett. 2020 Mar;594(5):924-932. doi: 10.1002/1873-3468.13673. Epub 2019 Nov 27.

Abstract

The nucleotide binding protein 35 (Nbp35)/cytosolic Fe-S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe-S cluster assembly scaffold required for the maturation of Fe-S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe-S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal host Methanococcus maripaludis contains a [4Fe-4S] cluster that can be transferred to a [4Fe-4S] apoprotein. Deletion of mmp0704 from M. maripaludis does not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe-4S] cluster transfer protein in methanogenic archaea.

Keywords: Methanococcus maripaludis; ApbC; Nbp35; archaea; iron-sulfur cluster; methanogen.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism
  • Cell Nucleus / metabolism
  • Cytosol / metabolism
  • Gene Deletion
  • Iron-Sulfur Proteins / genetics
  • Iron-Sulfur Proteins / metabolism*
  • Methanococcus / genetics
  • Methanococcus / growth & development*
  • Methanococcus / metabolism
  • Phylogeny

Substances

  • Archaeal Proteins
  • Iron-Sulfur Proteins