Honda Naoko, Kim Hyun, Rimbara Emiko, Kato Atsushi, Shibayama Keigo, Mori Shigetarou
Department of Quality Assurance & Radiological Protection, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjyuku-ku, Tokyo 162-8640, Japan.
Department of Bacteriology II, National Institute of Infectious Diseases, Gakuen 4-7-1, Musashimurayama-shi, Tokyo 208-0011, Japan.
Protein Expr Purif. 2015 Aug;112:37-42. doi: 10.1016/j.pep.2015.04.010. Epub 2015 Apr 30.
We recently demonstrated that the Rv2613c protein from Mycobacterium tuberculosis H37Rv is a novel diadenosine 5',5‴-P(1),P(4)-tetraphosphate (Ap4A) phosphorylase (MtAPA) that forms a tetramer. Mycobacterium avium and Mycobacterium smegmatis express proteins named MAV_3489 and MSMEG_2932, respectively, that are homologous to MtAPA. Here we showed that the MAV_3489 and MSMEG_2932 proteins possess Ap4A phosphorylase activity and enzymatic properties similar to those of MtAPA. Furthermore, gel-filtration column chromatography revealed that MAV_3489 and MSMEG_2932 assembled into homotetramers in solution, indicating that they may also form unique Ap4A-binding sites composed of tetramers.
我们最近证明，来自结核分枝杆菌H37Rv的Rv2613c蛋白是一种新型的二腺苷5',5‴-P(1),P(4)-四磷酸（Ap4A）磷酸化酶（MtAPA），它能形成四聚体。鸟分枝杆菌和耻垢分枝杆菌分别表达与MtAPA同源的名为MAV_3489和MSMEG_2932的蛋白。在此我们表明，MAV_3489和MSMEG_2932蛋白具有Ap4A磷酸化酶活性以及与MtAPA相似的酶学性质。此外，凝胶过滤柱层析显示MAV_3489和MSMEG_2932在溶液中组装成同型四聚体，这表明它们也可能形成由四聚体组成的独特的Ap4A结合位点。
