Structural and biophysical characterization of Mycobacterium tuberculosis dodecin Rv1498A

2011 ◽  
Vol 175 (1) ◽  
pp. 31-38 ◽  
Author(s):  
Fengxia Liu ◽  
Junhui Xiong ◽  
Sundaramurthy Kumar ◽  
Chunyan Yang ◽  
Shengxiang Ge ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Biophysical Characterization

scholarly journals Clinically relevant mutations of mycobacterial GatCAB inform regulation of translational fidelity

2021 ◽  
Author(s):  
Yang-Yang Li ◽  
Rong-Jun Cai ◽  
Jia-Ying Yang ◽  
Tamara L. Hendrickson ◽  
Ye Xiang ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Second Step ◽  
Loss Of Function ◽  
Wild Type ◽  
Translational Fidelity ◽  
Partial Loss ◽  
Biophysical Characterization ◽  
Minimal Impact ◽  
Mutant Strains

AbstractMost bacteria employ a two-step indirect tRNA aminoacylation pathway for the synthesis of aminoacylated tRNAGln and tRNAAsn. The heterotrimeric enzyme GatCAB performs a critical amidotransferase reaction in the second step of this pathway. We have previously demonstrated in mycobacteria that this two-step pathway is error-prone and translational errors contribute to adaptive phenotypes such as antibiotic tolerance. Furthermore, we identified clinical isolates of the globally important pathogen Mycobacterium tuberculosis with partial loss-of-function mutations in gatA, and demonstrated that these mutations result in high, specific rates of translational error and increased rifampicin tolerance. However, the mechanisms by which these clinically-derived mutations in gatA impact GatCAB function was unknown. Here, we describe biochemical and biophysical characterization of M. tuberculosis GatCAB, containing either wild-type gatA or one of two gatA mutants from clinical strains. We show that these mutations have minimal impact on enzymatic activity of GatCAB; however, they result in destabilization of the GatCAB complex as well as that of the ternary asparaginyl-transamidosome. Stabilizing complex formation with the solute trehalose increases specific translational fidelity of not only the mutant strains, but also of wild-type mycobacteria. Therefore, our data suggest that alteration of GatCAB stability may be a mechanism for modulation of translational fidelity.

Structural and biophysical characterization of Rv3716c, a hypothetical protein from Mycobacterium tuberculosis

2018 ◽  
Vol 495 (1) ◽  
pp. 982-987
Author(s):  
A. Gopalan ◽  
G. Deka ◽  
M. Prabhavathi ◽  
H.S. Savithri ◽  
M.R.N. Murthy ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Hypothetical Protein ◽  
Biophysical Characterization

scholarly journals Biophysical Characterization of the Tandem FHA Domain Regulatory Module from the Mycobacterium tuberculosis ABC Transporter Rv1747

Structure ◽  
2018 ◽  
Vol 26 (7) ◽  
pp. 972-986.e6 ◽  
Author(s):  
Florian Heinkel ◽  
Leo Shen ◽  
Melissa Richard-Greenblatt ◽  
Mark Okon ◽  
Jennifer M. Bui ◽  
...  
Keyword(s):  
Mycobacterium Tuberculosis ◽  
Abc Transporter ◽  
Fha Domain ◽  
Biophysical Characterization ◽  
Regulatory Module
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