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Rv2477c is an antibiotic-sensitive manganese-dependent ABC-F ATPase in Mycobacterium tuberculosis.

Abstract：

:The Rv2477c protein of Mycobacterium tuberculosis (Mtb) belongs to the ATP-binding cassette (ABC) subfamily F that contains proteins with tandem nucleotide-binding domains but lacking transmembrane domains. ABC-F subfamily proteins have been implicated in diverse cellular processes such as translation, antibiotic resistance, cell growth and nutrient sensing. In order to investigate the biochemical characteristics of Rv2477c, we expressed it in Escherichia coli, purified it and characterized its enzymatic functions. We show that Rv2477c displays strong ATPase activity (Vmax = 45.5 nmol/mg/min; Km = 90.5 μM) that is sensitive to orthovanadate. The ATPase activity was maximal in the presence of Mn2+ at pH 5.2. The Rv2477c protein was also able to hydrolyze GTP, TTP and CTP but at lower rates. Glutamate to glutamine substitutions at amino acid residues 185 and 468 in the two Walker B motifs of Rv2477c severely inhibited its ATPase activity. The antibiotics tetracycline and erythromycin, which target protein translation, were able to inhibit the ATPase activity of Rv2477c. We postulate that Rv2477c could be involved in mycobacterial protein translation and in resistance to tetracyclines and macrolides. This is the first report of the biochemical characterization of an ABC-F subfamily protein in Mtb.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Daniel J,Abraham L,Martin A,Pablo X,Reyes S

doi

10.1016/j.bbrc.2017.10.168

subject

Has Abstract

pub_date

2018-01-01 00:00:00

pages

35-40

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(17)32156-3

journal_volume

495

pub_type

杂志文章

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