Structural and thermodynamic characterization of a highly stable conformation of Rv2966c, a 16S rRNA methyltransferase, at low pH

Khan, Sabab Hasan; Bijpuria, Shipra; Maurya, Anjali; Taneja, Bhupesh

doi:10.1016/j.ijbiomac.2020.08.236

Cited by 3 publications

(1 citation statement)

References 53 publications

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“…Proteins of intracellular pathogens like M. tuberculosis have often been shown to have higher stability to retain their function in vivo ( 56 , 57 ). We examined whether the C-terminal tail of Ms_orn could play such a role to enable higher stability to the protein by thermal and Gdm-HCl–induced denaturation experiments.…”

Section: Discussionmentioning

confidence: 99%

Three-dimensional structure of a mycobacterial oligoribonuclease reveals a unique C-terminal tail that stabilizes the homodimer

Badhwar¹,

Khan²,

Taneja³

2022

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Three-dimensional structure of a mycobacterial oligoribonuclease reveals a unique C-terminal tail that stabilizes the homodimer

Badhwar¹,

Khan²,

Taneja³

2022

Journal of Biological Chemistry

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Epigenetic changes in Mycobacterium tuberculosis and its host provide potential targets or biomarkers for drug discovery and clinical diagnosis

Sui

Qiao

Xiang

et al. 2022

Pharmacological Research

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RNA Expression Analysis of Mycobacterial Methyltransferases Genes in Different Resistant Strains of Mycobacterium tuberculosis

Tarashi

Zamani

Bahramali

et al. 2022

ibj

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Background: Tuberculosis infection still represents a global health issue affecting patients worldwide. Strategies for its control may be not as effective as it should be, specifically in case of resistant strains of M.tb . In this regard, the role of mycobacterial MTases in TB infection can be fundamental, though it has not been broadly deciphered. Methods: Five resistant isolates of M.tb were obtained. M.tb H37Rv (ATCC 27249) was used as a reference strain. Seven putative mycobacterial MTase genes ( Rv0645c , Rv2966c , Rv1988 , Rv1694 , Rv3919c , Rv2756c , and Rv3263 ) and Rv1392 as SAM synthase were selected for analysis. PCR-sequencing and qRT-PCR were performed to compare mutations and expression levels of MTases in different strains. The 2 -ΔΔCt method was employed to calculate the relative expression levels of these genes. Results: Only two mutations were found in INH R strain for Rv3919c (T to G in codon 341) and Rv1392 (G to A in codon 97) genes. Overexpression of Rv0645c , Rv2756c , Rv3263 , and Rv2966c was detected in all sensitive and resistant isolates. However, Rv1988 and Rv3919c decreased and Rv1694 increased in the sensitive strains. The Rv1392 expression level also decreased in INH R isolate. Conclusion: We found a correlation between mycobacterial MTases expression and resistance to antibiotics in M.tb strains. Some MTases undeniably are virulence factors that specifically hijack the host defense mechanism. Further evaluations are needed to explore the complete impact of mycobacterial MTases within specific strains of M.tb to introduce novel diagnosis and treatment strategies.

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Structural and thermodynamic characterization of a highly stable conformation of Rv2966c, a 16S rRNA methyltransferase, at low pH

Cited by 3 publications

References 53 publications

Three-dimensional structure of a mycobacterial oligoribonuclease reveals a unique C-terminal tail that stabilizes the homodimer

Three-dimensional structure of a mycobacterial oligoribonuclease reveals a unique C-terminal tail that stabilizes the homodimer

Epigenetic changes in Mycobacterium tuberculosis and its host provide potential targets or biomarkers for drug discovery and clinical diagnosis

RNA Expression Analysis of Mycobacterial Methyltransferases Genes in Different Resistant Strains of Mycobacterium tuberculosis

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