Cross-linked amino acids in the protein pairs L3-L19 and L23-L29 of Bacillus stearothermophilus ribosomes after treatment with diepoxybutane.
作者： S. Herwig , V. Kruft , K. Eckart , B. Wittmann-Liebold
DOI: 10.1016/S0021-9258(18)53444-X
关键词: Ribosomal RNA 、 Ribosomal protein 、 Peptide sequence 、 Biology 、 Ribosome 、 Diepoxybutane 、 Sequence analysis 、 Biochemistry 、 Amino acid 、 Escherichia coli
摘要: Treatment of native 50 S ribosomal subunits Bacillus stearothermophilus with the homobifunctional cross-linking reagent diepoxybutane generated two cross-linked protein pairs, L3-L19 and L23-L29, which were isolated identified. The analysis sites at amino acid level in both pairs is presented. Using a combination sequence mass spectrometry it could be demonstrated that His-28 L3 N-terminal acids Met-1, His-2, His-3 L19 are involved forming cross-link L3-L19. Within pair L23-L29 Met-1 L23 Lys-4 L29 identified as employing similar approach. Comparison our data results derived from other experiments showed general structural organization ribosomes eubacteria (the Gram-positive B. Gram-negative Escherichia coli) has been conserved to quite an extent during evolution but fine structures differ slightly. By specificity its cleaving mechanism using sodium periodate examined. In addition complete determined revealed 58% identical residues homologous E. coli L19.
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