This title appears in the Scientific Report :
2016
Please use the identifier:
http://hdl.handle.net/2128/10428 in citations.
Please use the identifier: http://dx.doi.org/10.1073/pnas.1514529113 in citations.
The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin
The pupylation machinery is involved in iron homeostasis by targeting the iron storage protein ferritin
The balance of sufficient iron supply and avoidance of iron toxicity by iron homeostasis is a prerequisite for cellular metabolism and growth. Here we provide evidence that, in Actinobacteria, pupylation plays a crucial role in this process. Pupylation is a posttranslational modification in which th...
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Personal Name(s): | Küberl, Andreas |
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Polen, Tino (Corresponding author) / Bott, Michael (Corresponding author) | |
Contributing Institute: |
Biotechnologie; IBG-1 |
Published in: | Proceedings of the National Academy of Sciences of the United States of America, 113 (2016) 17, S. 4806 - 4811 |
Imprint: |
Washington, DC
National Acad. of Sciences
2016
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PubMed ID: |
27078093 |
DOI: |
10.1073/pnas.1514529113 |
Document Type: |
Journal Article |
Research Program: |
Biotechnology |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1073/pnas.1514529113 in citations.
The balance of sufficient iron supply and avoidance of iron toxicity by iron homeostasis is a prerequisite for cellular metabolism and growth. Here we provide evidence that, in Actinobacteria, pupylation plays a crucial role in this process. Pupylation is a posttranslational modification in which the prokaryotic ubiquitin-like protein Pup is covalently attached to a lysine residue in target proteins, thus resembling ubiquitination in eukaryotes. Pupylated proteins are recognized and unfolded by a dedicated AAA+ ATPase (Mycobacterium proteasomal AAA+ ATPase; ATPase forming ring-shaped complexes). In Mycobacteria, degradation of pupylated proteins by the proteasome serves as a protection mechanism against several stress conditions. Other bacterial genera capable of pupylation such as Corynebacterium lack a proteasome, and the fate of pupylated proteins is unknown. We discovered that Corynebacterium glutamicum mutants lacking components of the pupylation machinery show a strong growth defect under iron limitation, which was caused by the absence of pupylation and unfolding of the iron storage protein ferritin. Genetic and biochemical data support a model in which the pupylation machinery is responsible for iron release from ferritin independent of degradation. |