PMID:2505863
| Citation |
Chiaruttini, C, Milet, M, Hayes, DH and Expert-Bezancon, A (1989) Crosslinking of ribosomal proteins S4, S5, S7, S8, S11, S12 and S18 to domains 1 and 2 of 16S rRNA in the Escherichia coli 30S particle. Biochimie 71:839-52 |
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| Abstract |
RNA-protein crosslinks were introduced into Escherichia coli 30S ribosomal subunits by treatment with 1-ethyl-3(3-dimethylaminopropyl)carbodiimide (EDC). Complexes of 16S rRNA cross-linked to 30S ribosomal proteins were isolated and hybridized with a series of single-stranded bacteriophage M13-rDNA probes. These probes, each carrying an inserted rDNA fragment, were used to select contiguous 16S rRNA sections covering all of domain 1 and the major part of domain 2 (starting at the 5'-P terminus and ending at nucleotide 869) and the proteins covalently linked to each of these sections were identified by 2-dimensional polyacrylamide gel electrophoresis. This procedure identified proteins S4, S5, S7, S8, S11, S12, and S18 as the species most efficiently crosslinked to domains 1 and 2 of 16S rRNA. These results are discussed in the light of current knowledge of the tertiary structure of 16S rRNA in the E. coli 30S ribosomal subunit. |
| Links | |
| Keywords |
Cross-Linking Reagents/pharmacology; DNA Probes; Electrophoresis; Escherichia coli/metabolism; Ethyldimethylaminopropyl Carbodiimide; Nucleic Acid Conformation; Nucleic Acid Hybridization; RNA, Ribosomal/metabolism; RNA, Ribosomal, 16S/metabolism; Ribosomal Proteins/metabolism |
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