Abstract:
UNLABELLED:Pupylation is a posttranslational modification peculiar to actinobacteria wherein proteins are covalently modified with a small protein called the prokaryotic ubiquitin-like protein (Pup). Like ubiquitination in eukaryotes, this phenomenon has been associated with proteasome-mediated protein degradation in mycobacteria. Here, we report studies of pupylation in a streptomycete that is phylogentically related to mycobacteria. We constructed mutants of Streptomyces coelicolor lacking PafA (Pup ligase), the proteasome, and the Pup-proteasome system. We found that these mutants share a high susceptibility to oxidative stress compared to that of the wild-type strain. Remarkably, we found that the pafA null mutant has a sporulation defect not seen in strains lacking the Pup-proteasome system. In proteomics experiments facilitated by an affinity-tagged variant of Pup, we identified 110 pupylated proteins in S. coelicolor strains having and lacking genes encoding the 20S proteasome. Our findings shed new light on this unusual posttranslational modification and its role in Streptomyces physiology. IMPORTANCE:The presence of 20S proteasomes reminiscent of those in eukaryotes and a functional equivalent of ubiquitin, known as the prokaryotic ubiquitin-like protein (Pup), in actinobacteria have motivated reevaluations of protein homeostasis in prokaryotes. Though the Pup-proteasome system has been studied extensively in mycobacteria, it is much less understood in streptomycetes, members of a large genus of actinobacteria known for highly choreographed life cycles in which phases of morphological differentiation, sporulation, and secondary metabolism are often regulated by protein metabolism. Here, we define constituents of the pupylome in Streptomyces coelicolor for the first time and present new evidence that links pupylation and the oxidative stress response in this bacterium. Surprisingly, we found that the Pup ligase has a Pup-independent role in sporulation.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Compton CL,Fernandopulle MS,Nagari RT,Sello JKdoi
10.1128/JB.00302-15subject
Has Abstractpub_date
2015-09-01 00:00:00pages
2747-53issue
17eissn
0021-9193issn
1098-5530pii
JB.00302-15journal_volume
197pub_type
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.172.12.6727-6735.1990
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.177.12.3587-3588.1995
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
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pub_type: 杂志文章
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pub_type: 杂志文章
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更新日期:1967-08-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:2005-10-01 00:00:00
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更新日期:2001-03-01 00:00:00
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journal_title:Journal of bacteriology
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journal_title:Journal of bacteriology
pub_type: 杂志文章
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更新日期:1997-09-01 00:00:00
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journal_title:Journal of bacteriology
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更新日期:2005-01-01 00:00:00
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journal_title:Journal of bacteriology
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doi:10.1128/JB.146.2.527-534.1981
更新日期:1981-05-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.01527-06
更新日期:2007-03-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/jb.171.8.4410-4416.1989
更新日期:1989-08-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.154.3.1329-1338.1983
更新日期:1983-06-01 00:00:00
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journal_title:Journal of bacteriology
pub_type: 杂志文章
doi:10.1128/JB.163.3.1060-1066.1985
更新日期:1985-09-01 00:00:00