AI Article Synopsis
- - Mycobacterium tuberculosis (M. tb) has a unique cell wall structure primarily made of mycolic acids, which are important for its stability.
- - The desaturase A1 (DesA1) protein is vital for producing mycolic acids and requires calcium (Ca) for its function; mutations that disrupt Ca binding significantly affect the protein's performance.
- - Experiments showed that strains of Mycobacterium smegmatis with mutated DesA1 that can’t bind Ca exhibited poor growth and increased cell wall permeability, emphasizing the importance of Ca for Mycobacterium's cellular integrity.
Article Abstract
Mycobacterium tuberculosis (M. tb) has a complex cell wall, composed largely of mycolic acids, that are crucial to its structural maintenance. The M. tb desaturase A1 (DesA1) is an essential Ca-binding protein that catalyses a key step in mycolic acid biosynthesis. To investigate the structural and functional significance of Ca binding, we introduced mutations at key residues in its Ca-binding βγ-crystallin motif to generate DesA1F303A, E304Q, and F303A-E304Q. Complementation of a conditional ΔdesA1 strain of Mycobacterium smegmatis, with the Ca non-binders F303A or F303A-E304Q, failed to rescue its growth phenotype; these complements also exhibited enhanced cell wall permeability. Our findings highlight the criticality of Ca in DesA1 function, and its implicit role in the maintenance of mycobacterial cellular integrity.
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| http://dx.doi.org/10.1002/1873-3468.14896 | DOI Listing |
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