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Mycobacterium tuberculosis  is the causative agent of tuberculosis and has evolved an ability to survive in hostile host environments.  M .  tuberculosis  is thought to utilize the rTCA cycle to sustain its latent growth during infection, but the enzymatic characteristics and physiological function for the key citrate lyase of the rTCA cycle, MtbCitE, in the important pathogen remain unclear. In this study, we investigated the function of MtbCitE based on its structural properties and sequence comparisons with other bacterial citrate lyase subunits. We showed that several amino acid residues were important for the citrate cleavage activity of MtbCitE. Strikingly, the citrate cleavage activity of MtbCitE was inhibited by ATP, indicating that energy metabolism might couple with the regulation of MtbCitE activity, which differed from other CitEs. More interestingly, deletion of  citE  from  Mycobacterium bovis  BCG decreased the mycobacterial survival rate under hypoxic conditions, whereas complementation with  citE  restored the phenotype to wild-type levels. Consistently, three key rTCA cycle enzymes were positively regulated under hypoxic conditions in mycobacteria. Therefore, we characterized a unique citrate lyase MtbCitE from  M .  tuberculosis  and found that the CitE protein significantly contributed to mycobacterial survival under hypoxic conditions.

Citrate lyase CitE in Mycobacterium tuberculosis contributes to mycobacterial survival under hypoxic conditions