Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon <i>Haloferax volcanii</i>

<table>Rio-type protein kinases of <i>H. volcanii</i>. (a) Rio-type protein kinase homologs of <i>H. volcanii</i>, type-1 (HVO_0135) and type<b>-</b>2<b>-</b>like (HVO_0569), with conserved amino acid residues in bold and underlined. While HVO_0569 does not have a complete C-terminal domain, it does contain three of the five conserved residues of Rio type-2 kinases. (b) Purification of Rio1p (HVO_0135) from <i>H. volcanii</i>. Reducing SDS-PAGE gel of cell lysate (lane 1) and Rio1p purified by StrepTactin chromatography (lane 2) from in <i>H. volcanii</i>-pJAM2558. (c) Rio1p catalyzes its autophosphorylation. Autophosphotransfer was detected <i>in vitro</i> by autoradiography using [<svg height="20.275" id="M156" style="vertical-align:-3.56265pt" version="1.1" viewbox="0 0 39.137501 20.275" width="39.137501" xmlns="http://www.w3.org/2000/svg" xmlns:xlink="http://www.w3.org/1999/xlink">
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</svg>] ATP as a substrate with optimal activity detected at 10 to 50 mM MgCl<sub>2</sub>. *, identity of band remains to be determined.</table>

Archaea

fig3

Figure 3

Figure 3: Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon <i>Haloferax volcanii</i> 

Archaea

Phosphorylation and Methylation of Proteasomal Proteins of the Haloarcheon Haloferax volcanii

Figure 3