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| Status |
Public on Nov 01, 2024 |
| Title |
Identification of a depupylation regulator for an essential enzyme in Mycobacterium tuberculosis |
| Organism |
Mycobacterium tuberculosis |
| Experiment type |
Expression profiling by high throughput sequencing
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| Summary |
Mycobacterium tuberculosis can use a proteasome to degrade proteins when they are post-translationally modified with prokaryotic ubiquitin-like protein (Pup). While pupylation is reversible, mechanisms regulating depupylation have not been identified. Here, we identify a depupylation regulator, CoaX, a pseudo-pantothenate kinase. Pantothenate synthesis enzymes were more abundant in a ∆coaX mutant, including PanB, a substrate of the Pup-proteasome system. Media supplementation with pantothenate decreased PanB levels in a coaX and Pup-proteasome system-dependent manner. In vitro, CoaX accelerated depupylation of Pup~PanB, while addition of pantothenate inhibited this reaction. Collectively, we propose CoaX contributes to proteasomal degradation of PanB by modulating depupylation of Pup~PanB in response to pantothenate levels.
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| Overall design |
RNA was extracted from quadruplicate biological cultures of H37Rv pMV strep ev (WT with an empty vector, MHD761), coaX::hyg pMV strep ev (∆coaX with an empty vector, MHD1845), and coaX::hyg pMV strep coaX (complemented strain, MHD1846) of Mycobacterium tuberculosis (10 OD equivalents).
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| Contributor(s) |
Kahne SC, Darwin KH, Pironti A |
| Citation missing |
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| |
| Submission date |
Mar 04, 2024 |
| Last update date |
Nov 01, 2024 |
| Contact name |
Shoshanna Celia Kahne |
| E-mail(s) |
[email protected]
|
| Organization name |
New York University Grossman School of Medicine
|
| Department |
Microbiology
|
| Lab |
Heran Darwin
|
| Street address |
430 E 29th Street, Lab 324 C-D
|
| City |
New York |
| State/province |
NY |
| ZIP/Postal code |
10016 |
| Country |
USA |
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| Platforms (1) |
| GPL27507 |
Illumina NovaSeq 6000 (Mycobacterium tuberculosis) |
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| Samples (12)
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| Relations |
| BioProject |
PRJNA1083595 |
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