Use of the Novel Fluorescent Amino Acidp-Cyanophenylalanine Offers a Direct Probe of Hydrophobic Core Formation during the Folding of the N-Terminal Domain of the Ribosomal Protein L9 and Provides Evidence for Two-State Folding†

Biochemistry ◽  
2007 ◽  
Vol 46 (43) ◽  
pp. 12308-12313 ◽  
Author(s):  
Konstantinos N. Aprilakis ◽  
Humeyra Taskent ◽  
Daniel P. Raleigh
Keyword(s):  
Ribosomal Protein ◽  
The Novel ◽  
Hydrophobic Core ◽  
Core Formation ◽  
Terminal Domain ◽  
Ribosomal Protein L9

scholarly journals Structural Basis for the C-Terminal Domain of Mycobacterium tuberculosis Ribosome Maturation Factor RimM to Bind Ribosomal Protein S19

Biomolecules ◽  
2021 ◽  
Vol 11 (4) ◽  
pp. 597
Author(s):  
Haoran Zhang ◽  
Qiuxiang Zhou ◽  
Chenyun Guo ◽  
Liubin Feng ◽  
Huilin Wang ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Ribosomal Protein ◽  
Solution Structure ◽  
Molecular Mechanisms ◽  
Structural Model ◽  
Ribosomal Subunit ◽  
Structural Basis ◽  
Hydrophobic Core ◽  
Terminal Domain ◽  
Ribosomal Protein S19

Multidrug-resistant tuberculosis (TB) is a serious threat to public health, calling for the development of new anti-TB drugs. Chaperon protein RimM, involved in the assembly of ribosomal protein S19 into 30S ribosomal subunit during ribosome maturation, is a potential drug target for TB treatment. The C-terminal domain (CTD) of RimM is primarily responsible for binding S19. However, both the CTD structure of RimM from Mycobacterium tuberculosis (MtbRimMCTD) and the molecular mechanisms underlying MtbRimMCTD binding S19 remain elusive. Here, we report the solution structure, dynamics features of MtbRimMCTD, and its interaction with S19. MtbRimMCTD has a rigid hydrophobic core comprised of a relatively conservative six-strand β-barrel, tailed with a short α-helix and interspersed with flexible loops. Using several biophysical techniques including surface plasmon resonance (SPR) affinity assays, nuclear magnetic resonance (NMR) assays, and molecular docking, we established a structural model of the MtbRimMCTD–S19 complex and indicated that the β4-β5 loop and two nonconserved key residues (D105 and H129) significantly contributed to the unique pattern of MtbRimMCTD binding S19, which might be implicated in a form of orthogonality for species-dependent RimM–S19 interaction. Our study provides the structural basis for MtbRimMCTD binding S19 and is beneficial to the further exploration of MtbRimM as a potential target for the development of new anti-TB drugs.

scholarly journals The N-Terminal Domain of Ribosomal Protein L9 Folds via a Diffuse and Delocalized Transition State

2017 ◽  
Vol 112 (9) ◽  
pp. 1797-1806 ◽  
Author(s):  
Satoshi Sato ◽  
Jae-Hyun Cho ◽  
Ivan Peran ◽  
Rengin G. Soydaner-Azeloglu ◽  
Daniel P. Raleigh
Keyword(s):  
Transition State ◽  
Ribosomal Protein ◽  
Terminal Domain ◽  
Ribosomal Protein L9

Structure and Stability of the N-Terminal Domain of the Ribosomal Protein L9:  Evidence for Rapid Two-State Folding†

Biochemistry ◽  
1998 ◽  
Vol 37 (4) ◽  
pp. 1025-1032 ◽  
Author(s):  
Brian Kuhlman ◽  
Judith A. Boice ◽  
Robert Fairman ◽  
Daniel P. Raleigh
Keyword(s):  
Ribosomal Protein ◽  
Structure And Stability ◽  
Terminal Domain ◽  
Ribosomal Protein L9
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