A-Type Carrier Proteins Are Involved in [4Fe-4S] Cluster Insertion into the Radical S -Adenosylmethionine Protein MoaA for the Synthesis of Active Molybdoenzymes-Reference-Cited by-同舟云学术

A-Type Carrier Proteins Are Involved in [4Fe-4S] Cluster Insertion into the Radical S -Adenosylmethionine Protein MoaA for the Synthesis of Active Molybdoenzymes

Published:2021-05-20 Issue:12 Volume:203 Page:
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Hasnat Muhammad Abrar¹,Zupok Arkadiusz¹,Olas Justyna Jadwiga²,Mueller-Roeber Bernd²,Leimkühler Silke¹

Affiliation:

1. Institute of Biochemistry and Biology, Department of Molecular Enzymology, University of Potsdam, Potsdam, Germany

2. Institute of Biochemistry and Biology, Department of Molecular Biology, University of Potsdam, Potsdam, Germany

Abstract

Understanding the assembly of iron-sulfur (Fe-S) proteins is relevant to many fields, including nitrogen fixation, photosynthesis, bioenergetics, and gene regulation. Remaining critical gaps in our knowledge include how Fe-S clusters are transferred to their target proteins and how the specificity in this process is achieved, since different forms of Fe-S clusters need to be delivered to structurally highly diverse target proteins.

Funder

Deutsche Forschungsgemeinschaft

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.00086-21

Reference68 articles.

1. Mechanisms of iron–sulfur protein maturation in mitochondria, cytosol and nucleus of eukaryotes

2. Iron/sulfur proteins biogenesis in prokaryotes: Formation, regulation and diversity

3. Fe-S Cluster Assembly Pathways in Bacteria