Dissecting the Ca2+ dependence of DesA1 function in Mycobacterium tuberculosis.
FEBS Lett
; 598(13): 1620-1632, 2024 Jul.
Article
em En
| MEDLINE
| ID: mdl-38697952
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 Ca2+-binding protein that catalyses a key step in mycolic acid biosynthesis. To investigate the structural and functional significance of Ca2+ binding, we introduced mutations at key residues in its Ca2+-binding ßγ-crystallin motif to generate DesA1F303A, E304Q, and F303A-E304Q. Complementation of a conditional ΔdesA1 strain of Mycobacterium smegmatis, with the Ca2+ 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 Ca2+ in DesA1 function, and its implicit role in the maintenance of mycobacterial cellular integrity.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Parede Celular
/
Cálcio
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Mycobacterium tuberculosis
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Índia