<i>Rhodococcus</i>Prokaryotic Ubiquitin-Like Protein (Pup) Is Degraded by Deaminase of Pup (Dop)

Yun, Hea-Yeon; Tamura, Noriko; Tamura, Tomohide

doi:10.1271/bbb.120458

Cited by 11 publications

(16 citation statements)

References 33 publications

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“…The differences in the phenotypes of the pup and proteasome mutants observed in our study indicate that pupylation may have other roles in addition to its known proteasome-associated function. This conclusion is consistent with previous observations (26,29) that not all pupylated proteins are degraded. Furthermore, pupylation occurs in corynebacteria, which do not have a proteasome (30).…”

Section: Figsupporting

confidence: 94%

“…The functional group most frequently identified was posttranslational modification, protein turnover, and chaperone functions (O); four of the pupylation target proteins belonged to this group. Orthologues of seven of the 20 proteins (AcpP, FabF, PurA, Tuf1, GroEL1, AhpC, and SCO6042) were also identified in at least one of the pupylomes reported for M. tuberculosis, M. smegmatis, R. erythropolis, or C. glutamicum (26)(27)(28)(29)(30). However, 10 proteins pupylated in S. coelicolor were not described in any of the mycobacterial, Rhodococcus, and Corynebacterium pupylome analyses despite their conservation in these genera.…”

Section: Expression Of Pupylation and Proteasome Genes In S Coelicolormentioning

confidence: 92%

“…We identified 20 pupylation targets in S. coelicolor. Seven of these target proteins have homologues that are also pupylated in Mycobacterium, R. erythropolis, or C. glutamicum (26)(27)(28)(29)(30). These homologous proteins were, in some cases, modified at different positions in different actinobacteria (see Fig.…”

Section: Figmentioning

confidence: 99%

“…Pupylation was also demonstrated in Rhodococcus erythropolis (29) and in Corynebacterium glutamicum (30), and proteins targeted by pupylation in these organisms have been identified. Pupylated targets are numerous and belong to various functional classes of proteins.…”

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confidence: 93%

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The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor

et al. 2015

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Protein turnover is essential in all living organisms for the maintenance of normal cell physiology. In eukaryotes, most cellular protein turnover involves the ubiquitin-proteasome pathway, in which proteins tagged with ubiquitin are targeted to the proteasome for degradation. In contrast, most bacteria lack a proteasome but harbor proteases for protein turnover. However, some actinobacteria, such as mycobacteria, possess a proteasome in addition to these proteases. A prokaryotic ubiquitination-like tagging process in mycobacteria was described and was named pupylation: proteins are tagged with Pup (prokaryotic ubiquitin-like protein) and directed to the proteasome for degradation. We report pupylation in another actinobacterium, Streptomyces coelicolor. Both the morphology and life cycle of Streptomyces species are complex (formation of a substrate and aerial mycelium followed by sporulation), and these bacteria are prolific producers of secondary metabolites with important medicinal and agricultural applications. The genes encoding the pupylation system in S. coelicolor are expressed at various stages of development. We demonstrated that pupylation targets numerous proteins and identified 20 of them. Furthermore, we established that abolition of pupylation has substantial effects on morphological and metabolic differentiation and on resistance to oxidative stress. In contrast, in most cases, a proteasome-deficient mutant showed only modest perturbations under the same conditions. Thus, the phenotype of the pup mutant does not appear to be due solely to defective proteasomal degradation. Presumably, pupylation has roles in addition to directing proteins to the proteasome. IMPORTANCEStreptomyces spp. are filamentous and sporulating actinobacteria, remarkable for their morphological and metabolic differentiation. They produce numerous bioactive compounds, including antifungal, antibiotic, and antitumor compounds. There is therefore considerable interest in understanding the mechanisms by which Streptomyces species regulate their complex physiology and production of bioactive compounds. We studied the role in Streptomyces of pupylation, a posttranslational modification that tags proteins that are then directed to the proteasome for degradation. We demonstrated that the absence of pupylation had large effects on morphological differentiation, antibiotic production, and resistance to oxidative stress in S. coelicolor. The phenotypes of pupylation and proteasome-defective mutants differed and suggest that pupylation acts in a proteasome-independent manner in addition to its role in proteasomal degradation.T urnover of cellular proteins is required in all living organisms to maintain normal cellular physiology. In eukaryotes, the ubiquitin-proteasome pathway is the major route of protein degradation and turnover (1). Ubiquitin is a 76-residue protein that can be conjugated to target proteins, marking them for degradation by the 26S proteasome complex. In addition to its role in tagging proteins for degradation...

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Section: Figsupporting

confidence: 94%

Section: Expression Of Pupylation and Proteasome Genes In S Coelicolormentioning

confidence: 92%

Section: Figmentioning

confidence: 99%

mentioning

confidence: 93%

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The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor

et al. 2015

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“…Indeed, like mitochondria being consumed to provide energy for a cell 13 weak herbivores were found in several bacteria (e.g., Pup in Mycobacterium tuberculosis, 18 and Samp proteins in Haloferax volcanii 18,19 ). In addition, prokaryotes also have an analog of deubiquitinases: a recent discovery of a deaminase of Pup (Dop), 20 which removes the Pup-tag from bacterial proteins, suggests that prokaryote proteolysis systems are as flexible as those found in eukaryotes.…”

Section: Autophagy Overviewmentioning

confidence: 99%

A bird’s-eye view of autophagy

Starokadomskyy

Dmytruk

2013

Autophagy

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Pupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis

et al. 2014

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In a manner similar to ubiquitin, the prokaryotic ubiquitin-like protein (Pup) has been shown to target proteins for degradation via the proteasome in mycobacteria. However, not all actinobacteria possessing the Pup protein also contain a proteasome. In this study, we set out to study pupylation in the proteasome-lacking non-pathogenic model organism Corynebacterium glutamicum. A defined pup deletion mutant of C. glutamicum ATCC 13032 grew aerobically as the parent strain in standard glucose minimal medium, indicating that pupylation is dispensable under these conditions. After expression of a Pup derivative carrying an aminoterminal polyhistidine tag in the Δpup mutant and Ni(2+)-chelate affinity chromatography, pupylated proteins were isolated. Multidimensional protein identification technology (MudPIT) and MALDI-TOF-MS/MS of the elution fraction unraveled 55 proteins being pupylated in C. glutamicum and 66 pupylation sites. Similar to mycobacteria, the majority of pupylated proteins are involved in metabolism or translation. Our results define the first pupylome of an actinobacterial species lacking a proteasome, confirming that other fates besides proteasomal degradation are possible for pupylated proteins.

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RhodococcusProkaryotic Ubiquitin-Like Protein (Pup) Is Degraded by Deaminase of Pup (Dop)

Cited by 11 publications

References 33 publications

The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor

The Absence of Pupylation (Prokaryotic Ubiquitin-Like Protein Modification) Affects Morphological and Physiological Differentiation in Streptomyces coelicolor

A bird’s-eye view of autophagy

Pupylated proteins in Corynebacterium glutamicum revealed by MudPIT analysis

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