RNA-protein interactions in the ribosome. Binding of 50-S-subunit proteins to 5' and 3' terminal segments of the 23-S RNA
| Autor: | Robert A. Zimmermann, George A. Mackie, Pierre Spierer |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Riboswitch
Ribosomal Proteins 5.8S ribosomal RNA Carrier Proteins/metabolism Biology Biochemistry Ribosome RNA Ribosomal/metabolism Ribonucleases ddc:590 Escherichia coli Signal recognition particle RNA Ribosomes/metabolism Oligoribonucleotides Base Sequence Intron Oligoribonucleotides/analysis RNA Molecular biology Molecular Weight Kinetics RNA editing RNA Ribosomal Transfer RNA Escherichia coli/metabolism Ribosomal Proteins/metabolism Carrier Proteins Ribosomes Protein Binding |
| Zdroj: | European Journal of Biochemistry, Vol. 52, No 3 (1975) pp. 459-68 |
| ISSN: | 0014-2956 |
| Popis: | Limited digestion of the Escherichia coli 50-S subunit permits the isolation of two large fragments of the 23-S RNA. One arises from the 5' end of the 23-S RNA and contains about 1200 nucleotides. The other arises from the 3' end of the 23-S RNA and contains about 2000 nucleotides. Each of the ten 50-S proteins known to bind specifically and independently to the 23-S RNA were tested for their ability to interact with these two RNA fragments. It was determined that the 5' terminal segment contains the specific binding sites for proteins L4, L20 and L24, whereas the 3' terminal segment contains the specific binding sites for proteins L1, L2, L3, L6, L13, L13 and L23. |
| Databáze: | OpenAIRE |
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