Related ArticlesFate of Pup inside the Mycobacterium Proteasome Studied by in-Cell NMR.
PLoS One. 2013;8(9):e74576
Authors: Maldonado AY, Burz DS, Reverdatto S, Shekhtman A
Abstract
The Mycobacterium tuberculosis proteasome is required for maximum virulence and to resist killing by the host immune system. The prokaryotic ubiquitin-like protein, Pup-GGE, targets proteins for proteasome-mediated degradation. We demonstrate that Pup-GGQ, a precursor of Pup-GGE, is not a substrate for proteasomal degradation. Using STINT-NMR, an in-cell NMR technique, we studied the interactions between Pup-GGQ, mycobacterial proteasomal ATPase, Mpa, and Mtb proteasome core particle (CP) inside a living cell at amino acid residue resolution. We showed that under in-cell conditions, in the absence of the proteasome CP, Pup-GGQ interacts with Mpa only weakly, primarily through its C-terminal region. When Mpa and non-stoichiometric amounts of proteasome CP are present, both the N-terminal and C-terminal regions of Pup-GGQ bind strongly to Mpa. This suggests a mechanism by which transient binding of Mpa to the proteasome CP controls the fate of Pup.
[NMR paper] Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Related Articles Multi-phosphorylation of the Intrinsically Disordered Unique Domain of c-Src Studied by In-Cell and Real-Time NMR Spectroscopy.
Chembiochem. 2013 Jun 6;
Authors: Amata I, Maffei M, Igea A, Gay M, Vilaseca M, Nebreda AR, Pons M
Abstract
Intrinsically disordered regions (IDRs) are preferred sites for post-translational modifications essential for regulating protein function. The enhanced local...
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[NMR paper] Protein dynamics in living cells studied by in-cell NMR spectroscopy.
Protein dynamics in living cells studied by in-cell NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Protein dynamics in living cells studied by in-cell NMR spectroscopy.
FEBS Lett. 2013 Jan 11;
Authors: Li C, Liu M
Abstract
Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques...
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Protein dynamics in living cells studied by in-cell NMR spectroscopy
Protein dynamics in living cells studied by in-cell NMR spectroscopy
Available online 11 January 2013
Publication year: 2013
Source:FEBS Letters</br>
</br>
Most proteins function in cells where protein concentrations can reach 400g/l. However, most quantitative studies of protein properties are performed in idealized, dilute conditions. Recently developed in-cell NMR techniques can provide protein structure and other biophysical properties inside living cells at atomic resolution. Here we review how protein dynamics, including global and internal motions have been...
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Methyl-TROSY NMR studies of proteasome allostery [Biophysics and Computational Biology]
Methyl-TROSY NMR studies of proteasome allostery
Ruschak, A. M., Kay, L. E....
Date: 2012-12-11
Protein degradation plays a critical role in cellular homeostasis, in regulating the cell cycle, and in the generation of peptides that are used in the immune response. The 20S proteasome core particle (CP), a barrel-like structure consisting of four heptameric protein rings stacked axially on top of each other, is... Read More
PNAS:
Number: 50
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Structure and Dynamicsof Mycobacterium tuberculosis Truncated HemoglobinN: Insights from NMR Spectroscopy and MolecularDynamics Simulations
Structure and Dynamicsof Mycobacterium tuberculosis Truncated HemoglobinN: Insights from NMR Spectroscopy and MolecularDynamics Simulations
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi201059a/aop/images/medium/bi-2011-01059a_0006.gif
Biochemistry
DOI: 10.1021/bi201059a
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/sSrnnNxPk8g
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[NMR paper] NMR assignment of protein Rv1980c from Mycobacterium tuberculosis.
NMR assignment of protein Rv1980c from Mycobacterium tuberculosis.
Related Articles NMR assignment of protein Rv1980c from Mycobacterium tuberculosis.
J Biomol NMR. 2005 Sep;33(1):73
Authors: Danahy JM, Potter BM, Geisbrecht BV, Laity JH
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Novel Small Molecule Inhibitors of MDR Mycobacterium tuberculosis by NMR Fragment Scr
Novel Small Molecule Inhibitors of MDR Mycobacterium tuberculosis by NMR Fragment Screening of Antigen 85C.
Related Articles Novel Small Molecule Inhibitors of MDR Mycobacterium tuberculosis by NMR Fragment Screening of Antigen 85C.
J Med Chem. 2010 Nov 12;
Authors: Scheich C, Puetter V, Schade M
Protein target-based discovery of novel antibiotics has been largely unsuccessful despite rich genome information. Particularly in need are new antibiotics for tuberculosis, which kills 1.6 million people annually and shows a rapid increase in...