SpkH (Sll0005) from Synechocystis sp. PCC 6803 is an active Mn2+-dependent Ser kinase

Zorina, A.A.; Novikova, G.V.; Gusev, N.B.; Leusenko, A.V.; Los, D.A.; Klychnikov, O.I.

Авторы: Zorina A.A., Novikova G.V., Gusev N.B., Leusenko A.V., Los D.A., Klychnikov O.I.
Журнал: Biochimie
Год издания: 2023
Издательство: Elsevier BV
Местоположение издательства: Netherlands
DOI: 10.1016/j.biochi.2023.05.006
Аннотация: Twelve genes for the potential serine-threonine protein kinases (STPKs) have been annotated in the genome of Synechocystis sp. PCC 6803. Based on similarities and distinctive domain organization, they were divided into two clusters: serine/threonine-protein N2-like kinases (PKN2-type) and “activity of bc1 complex” kinases (ABC1-type). While the activity of the PKN2-type kinases have been demonstrated, no ABC1-type kinases activity have hitherto been reported. In this study, a recombinant protein previously annotated as a potential STPK of ABC1-type (SpkH, Sll0005) was expressed and purified to homogeneity. We demonstrated SpkH phosphorylating activity and substrate preference for casein in in vitro assays using [γ-32P]ATP. Detailed analyses of activity showed that Mn2+ had the strongest activation effect. The activity of SpkH was significantly inhibited by heparin and spermine, but not by staurosporine. By means of semi-quantitative mass-spectrometric detection of phosphopeptides, we identified a consensus motif recognized by this kinase – X1X2pSX3E. Thus, we first report here that SpkH of Synechocystis represents a true active serine protein kinase, which shares the properties of casein kinases according to its substrate specificity and sensitivity to some activity effectors.Клычников О.И. КТУ - 3
Добавил в систему: Клычников Олег Игоревич

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SpkH (Sll0005) from Synechocystis sp. PCC 6803 is an active Mn2+-dependent Ser kinaseстатья Исследовательская статья

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