Nudix hydrolases with Coenzyme A (CoA) and acyl-CoA pyrophosphatase activities confer growth advantage to Mycobacterium smegmatis
| Autor: | Shashanka Aroli, Umesh Varshney, Rajagopal Varada, Indu Kapoor |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Microbiology & Cell Biology
chemistry.chemical_classification 0303 health sciences Pyrophosphatase biology 030306 microbiology Coenzyme A Mycobacterium smegmatis biology.organism_classification Microbiology Nudix hydrolase 03 medical and health sciences chemistry.chemical_compound Acyl-CoA chemistry Biochemistry Nucleotide Phosphopantetheine Nucleoside 030304 developmental biology |
| Zdroj: | Microbiology. 165:1219-1232 |
| ISSN: | 1465-2080 1350-0872 |
| DOI: | 10.1099/mic.0.000850 |
| Popis: | Nudix hydrolase family proteins hydrolyse toxic by-products of cellular metabolism such as mutagenic nucleoside triphosphates, sugar nucleotides and signalling molecules. We studied the substrate specificities of Nudix hydrolases encoded by rv3672c and rv3040c from Mycobacterium tuberculosis and their respective homologues, msmeg_6185 and msmeg_2327 from M. smegmatis. The rv3672c- and msmeg_6185-encoded proteins (Rv3672 and MSMEG_6185, respectively) showed CoA pyrophosphatase (CoAse) activity that converted acyl-CoA to adenosine-3',5'-diphosphate (3', 5'-ADP) and 4-acyl phosphopantetheine. The efficiencies of Rv3672 and MSMEG_6185 in hydrolysing CoA derivatives were found to be higher than those of the Rv3040 and MSMEG_2327 (encoded by rv3040c and msmeg_2327, respectively). Further, amongst the substrates tested, Rv3672 and MSMEG_6185 used CoA and oxidized CoA as the most preferred substrates. Use of the M. smegmatis model showed that the expression of msmeg_6185 occurs in the log and stationary phases but declines during the late stationary phase and becomes undetectable during hypoxia. The co-culture competition experiments performed between the wild-type and Delta msmeg_6185 strains of M. smegmatis in different carbon sources revealed that the presence of msmeg_6185 provided growth fitness advantage to M. smegmatis, irrespective of the carbon source, implicating its function in regulation for the optimal physiological levels of acyl-CoAs in the cell. |
| Databáze: | OpenAIRE |
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