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FilenameFormatSizeDescription
pmic7386-sup-0001-FigureS1.tif219KFigure S1. Peptide coverage of the MALDI-TOF analysis of the anti-GlnK reactive spots. Spots 1-3 show the GlnK1 sequence, spots 4-5 the one from GlnK2. The matched peptides are indicated in bold red; underlined peptides have different masses in the two GlnK homologues and permit differentiation of the two H. mediterranei homologues.
pmic7386-sup-0002-FigureS2.tif376KFigure S2. Alignment of different PII proteins showing the conservation of the family signature patterns and uridylylable tyrosine. Alignment performed with ClustalW2; (*) indicates positions which have a single, fully conserved residue, (:) means conserved amino acid change and (.) means semiconserved change. PII signature patterns are highlighted: yellow for PII protein uridylylation site (PS00496, PROSITE) with the uridylylable tyrosine framed; blue for PII protein C-terminal region signature (PS00638, PROSITE). Sequences: GlnK1 and GlnK2 from H. mediterranei (HM) (UniProtKB accession numbers B8ZYW0 and B8ZYW1), GlnK and GlnB from E. coli (EC) (P0AC55 and P0A9Z1) and GlnK1 from Methanosarcina mazei (MM) (Q8U4U3).
pmic7386-sup-0005-TableS1.ppt229KTable S1. Sequence accession numbers and theoretical physicochemical data for H. mediterranei GlnK proteins.
pmic7386-sup-0006-TableS2.ppt261KTable S2. Theoretical masses of the peptides obtained as product of a trypsin digestion of H. mediterranei GlnK proteins (no missed cleavages). Mass values in Dalton, site indicates the amino acid after which the polypeptide is cleaved.
pmic7386-sup-0004-supmat2.doc153KSuppoting Information

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