Involvement of lysine and arginine residues in the binding of yeast ribosomal protein YL3 to 5S RNA.
The contribution of lysine and arginine residues to the formation of yeast ribonucleoprotein complex 5S RNA. protein YL3 has been investigated by determining the effects on complex formation of modification with chemical reagents specific for either lysine or arginine. Treatment of protein YL3 with acetic anhydride, maleic anhydride or phenylglyoxal is accompanied by loss of its capacity to bind to 5S RNA. This effect is accomplished by modification with phenylglyoxal of only 3 arginine residues per YL3 molecule. In contrast, a large number of protein YL3 amino groups must be modified by acetic anhydride to prevent complex formation.
D000089:Acetic Anhydrides; D001120:Arginine / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism; D008239:Lysine / Q000378:metabolism*; D010658:Phenylglyoxal; D011485:Protein Binding; D012335:RNA, Ribosomal / Q000378:metabolism*; D012341:RNA, Ribosomal, 5S / Q000378:metabolism*; D012441:Saccharomyces cerevisiae
D000089:Acetic Anhydrides; D005656:Fungal Proteins; D012335:RNA, Ribosomal; D012341:RNA, Ribosomal, 5S; C031800:acetic anhydride; D001120:Arginine; D008239:Lysine; D010658:Phenylglyoxal