Multiple crosslinks of proteins S7 and S9 to domains 3 and 4 of 16S ribosomal RNA in the Escherichia coli 30S particle.
RNA-protein cross-links were introduced into Escherichia coli 30S subunits by treatment with 1-ethyl-3(3-dimethylaminopropyl)carbodiimide. 16S rRNA, cross-linked to 30S ribosomal proteins, was isolated and hybridized with seven single-stranded bacteriophage M13-DNA probes. These probes, each carrying an inserted rDNA fragment, were used to select contiguous RNA sections covering domains 3 and 4 (starting at nucleotide 868 and ending at the 3'OH terminus) of the 16S rRNA. The proteins covalently linked to each selected RNA section were identified by two-dimensional polyacrylamide gel electrophoresis. Proteins S7 and S9 were shown to be efficiently cross-linked to multiple sites belonging to both domains.
D001426:Bacterial Proteins / Q000032:analysis*; D001665:Binding Sites; D003432:Cross-Linking Reagents; D004926:Escherichia coli / Q000032:analysis*; D005022:Ethyldimethylaminopropyl Carbodiimide; D009693:Nucleic Acid Hybridization; D011485:Protein Binding; D012329:RNA, Bacterial / Q000032:analysis*; D012335:RNA, Ribosomal / Q000032:analysis*; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins / Q000032:analysis*
D001426:Bacterial Proteins; D003432:Cross-Linking Reagents; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D000091243:Ribosomal Protein S9; D012269:Ribosomal Proteins; C037442:ribosomal protein S7; D005022:Ethyldimethylaminopropyl Carbodiimide