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Deprecated: Implicit conversion from float 245.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Proc+Natl+Acad+Sci+U+S+A 2016 ; 113 (17): 4806-11 Nephropedia Template TP
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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 PMID27078093show ga
Pupylation is a posttranslational protein modification discovered in Mycobacterium tuberculosis in which it tags proteins for degradation via the proteasome. It thus resembles eukaryotic ubiquitination. In mycobacteria, pupylation plays a role under oxidative stress and under carbon and nitrogen starvation. Intriguingly, many bacteria containing the pupylation machinery lack a proteasome, such as corynebacteria, leaving the function of this protein modification open. We show that pupylation in Corynebacterium glutamicum plays a dedicated role in iron homeostasis by targeting the iron-storage protein ferritin. Evidence is provided that pupylation triggers the disassembly of 24-meric ferritin by ARC to support the release of the stored iron without using a protease. Thus, a physiological function of pupylation was discovered for a proteasome-free bacterial species.