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2016 ; 113
(17
): 4806-11
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The pupylation machinery is involved in iron homeostasis by targeting the iron
storage protein ferritin
#MMPMID27078093
Küberl A
; Polen T
; Bott M
Proc Natl Acad Sci U S A
2016[Apr]; 113
(17
): 4806-11
PMID27078093
show ga
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.