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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Zhao C,Lyu Z,Long F,Akinyemi T,Manakongtreecheep K,Söll D,Whitman WB,Vinyard DJ,Liu Y

doi

10.1002/1873-3468.13673

subject

Has Abstract

pub_date

2020-03-01 00:00:00

pages

924-932

issue

5

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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