Mycobacterium tuberculosis tyrosine phosphatase A (PtpA) activity is modulated by S-nitrosylation.
M. tuberculosis PtpA and PtpB, the only two phosphotyrosine phosphatases (Ptps) present in this pathogen, play an important role in mycobacteria survival inside macrophages. The aim of the present work was to investigate M. tuberculosis PtpA and PtpB susceptibility to S-nitrosylation, a reversible covalent bond between nitric oxide (NO) and specific cysteine (sulfur) residues in proteins. PtpB was not modified by NO, in contrast, PtpA Cys53 was identified by site directed mutagenesis as the target of S-nitrosylation.
Ecco
Gabriela
G
Centro de Biologia Molecular Estrutural, BQA CCB UFSC, Florianópolis-SC, Brazil.
Vernal
Javier
J
Razzera
Guilherme
G
Martins
Priscila Alves
PA
Matiollo
Camila
C
Terenzi
Hernán
H
D003545:Cysteine / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009169:Mycobacterium tuberculosis / Q000201:enzymology* / Q000235:genetics; D009569:Nitric Oxide / Q000378:metabolism*; D017027:Protein Tyrosine Phosphatases / Q000235:genetics / Q000378:metabolism*
D009569:Nitric Oxide; D017027:Protein Tyrosine Phosphatases; D003545:Cysteine