The Binding Site of Protein L1 on 23‐S Ribosomal RNA of Escherichia coil
Open Access
- 1 November 1976
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 70 (2) , 457-469
- https://doi.org/10.1111/j.1432-1033.1976.tb11037.x
Abstract
Ribonucleoproteins were obtained by T1 RNase [EC 3.1.4.8] digestion of reconstituted complexes of ribosomal protein L1 and 23-S RNA from E. coli. The RNA region of the main ribonucleoprotein 2 was totally digested with T1 RNase. The oligonucleotide products were characterized; this region comprises 148 nucleotides located 550-1000 nucleotides from the 3'' end of the 23-S RNA. Of the other 2 ribonucleotides the largest nucleoprotein 1 contained an extra RNA sequence of at least 15 nucleotides that was located at the 5'' end of the RNA region. The smallest ribonucleoprotein 3 lacked an RNA section towards the 3'' end of the region. The order of the RNA subfragments and the enzymic cutting positions in the whole RNA region are given for the ribonucleoproteins. Protein L1 most strongly protects a continuous section of 115 nucleotides at the 5'' end of the main RNA region. Evidence is presented for a methylated base and 2 sequence heterogeneities in this region of the 23-S RNA.This publication has 5 references indexed in Scilit:
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