Publication Date:
2008-10-04
Description:
The protein modifier ubiquitin is a signal for proteasome-mediated degradation in eukaryotes. Proteasome-bearing prokaryotes have been thought to degrade proteins via a ubiquitin-independent pathway. We have identified a prokaryotic ubiquitin-like protein, Pup (Rv2111c), which was specifically conjugated to proteasome substrates in the pathogen Mycobacterium tuberculosis. Pupylation occurred on lysines and required proteasome accessory factor A (PafA). In a pafA mutant, pupylated proteins were absent and substrates accumulated, thereby connecting pupylation with degradation. Although analogous to ubiquitylation, pupylation appears to proceed by a different chemistry. Thus, like eukaryotes, bacteria may use a small-protein modifier to control protein stability.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2698935/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2698935/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearce, Michael J -- Mintseris, Julian -- Ferreyra, Jessica -- Gygi, Steven P -- Darwin, K Heran -- 5T32AI07189-25/AI/NIAID NIH HHS/ -- AI065437/AI/NIAID NIH HHS/ -- GM67945/GM/NIGMS NIH HHS/ -- HG3456/HG/NHGRI NIH HHS/ -- HG3616/HG/NHGRI NIH HHS/ -- HL092774/HL/NHLBI NIH HHS/ -- R01 HL092774/HL/NHLBI NIH HHS/ -- R01 HL092774-01/HL/NHLBI NIH HHS/ -- R01 HL092774-02/HL/NHLBI NIH HHS/ -- R56 AI065437/AI/NIAID NIH HHS/ -- R56 AI065437-01A2/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2008 Nov 14;322(5904):1104-7. doi: 10.1126/science.1163885. Epub 2008 Oct 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, New York University School of Medicine, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18832610" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphatases/genetics/*metabolism
;
Amino Acid Motifs
;
Bacterial Proteins/chemistry/genetics/isolation & purification/*metabolism
;
Glutamic Acid/metabolism
;
Glutamine/metabolism
;
Glycine/metabolism
;
Lysine/metabolism
;
Mass Spectrometry
;
Molecular Sequence Data
;
Mutation
;
Mycobacterium smegmatis/metabolism
;
Mycobacterium tuberculosis/genetics/*metabolism
;
Proteasome Endopeptidase Complex/*metabolism
;
Recombinant Fusion Proteins/chemistry/metabolism
;
Ubiquitination
;
Ubiquitins/chemistry/genetics/isolation & purification/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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