Proteins associated with rRNA in the Escherichia coli ribosome.
Ribosomal proteins located near the rRNA have been identified by cross linking to [14C]spermine with 1,5-difluoro-2,4-dinitrobenzene. The polyamine binds to double-stranded rRNA; those proteins showing radioactivity covalently bound after treatment with the bifunctional reagent should therefore be located in the vicinity of these regions of rRNA. Six proteins from the small subunit, S4, S5, S9, S18, S19 and S20 and ten proteins from the large subunit L2, L6, L13, L14, L16, L17, L18, L19, L22 and L27 preferentially take up the label. The results obtained with three proteins from the large subunit, L6, L16 and L27, show a high degree of variability that could reflect differences of conformation in the subunit population. Several proteins were drastically modified by the cross-linking agent but were not detected in the two-dimensional gel electrophoresis (e.g., S1, S11, S21, L7, L8 and L12) and therefore could not be studied.
D004139:Dinitrofluorobenzene / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D008970:Molecular Weight; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000032:analysis / Q000378:metabolism*; D012270:Ribosomes / Q000378:metabolism; D013096:Spermine / Q000378:metabolism
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D013096:Spermine; D004139:Dinitrofluorobenzene