Towards understanding the biological function of the unusual chaperonin GroEL1 of Mycobacterium tuberculosis

ABSTRACT: Expression data from wild type (H37Rv) and GroEL1(H37RvΔgroEL1::Hyg) mutant strains under a range of environmental stresses The 60 kDa heat shock proteins, also known as GroELs are components of the essential protein folding machinery of the cell, but are also dominant antigens in many infectious diseases. Although generally essential for cellular survival, in some organisms such as Mycobacterium tuberculosis, one or more paralogous GroELs are known to be dispensable. In M. tuberculosis, groEL2 is essential for cell survival, but the biological role of the non-essential GroEL1 is still elusive. To understand the relevance of GroEL1 in M. tuberculosis physiology, detailed transcriptomic analyses for the wild type H37Rv and groEL1 knockout (groEL1 KO) were performed under in vitro stress conditions: stationary phase, cold shock, low aeration, mild cold shock and low pH. Additionally, the survival of the groEL1 KO was assessed in macrophages at multiplicity of infection (MOI) of 1:1 and 1:5. We observed that survival under low aeration was significantly compromised in the groEL1 KO. Further, the gene expression analyses under low aeration showed change in expression of several key virulence factors like two component system PhoP/R and MprA/B, sigma factors sigG, M and H and adversely affected known hypoxia response regulators Rv0081, Rv0023 and DosR. Our work is therefore suggestive of an important role of GroEL1 for survival under low aeration by affecting the expression of genes known for hypoxia response.

ORGANISM(S): Mycobacterium tuberculosis H37Rv

PROVIDER: GSE68856 | GEO | 2015/05/14

SECONDARY ACCESSION(S): PRJNA283909

REPOSITORIES: GEO