scholarly journals A possible role of the 5′terminal sequence of 16S ribosomal RNA In the recognltton of Initiation sequences for protein synthesis

1975 ◽  
Vol 2 (1) ◽  
pp. 79-86 ◽  
Author(s):  
P.H. van Knlppenberg
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Rna ◽  
16S Ribosomal Rna ◽  
Terminal Sequence

scholarly journals Identical 3′-terminal octanucleotide sequence in 18S ribosomal ribonucleic acid from different eukaryotes. A proposed role for this sequence in the recognition of terminator codons

1974 ◽  
Vol 141 (3) ◽  
pp. 609-615 ◽  
Author(s):  
John Shine ◽  
Lynn Dalgarno
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Synthesis ◽  
Drosophila Melanogaster ◽  
Ribosomal Rna ◽  
Ribonucleic Acid ◽  
18S Rrna ◽  
Base Sequence ◽  
Terminal Sequence ◽  
Ribosomal Ribonucleic Acid ◽  
Rrna Species

The 3′-terminal sequence of 18S ribosomal RNA from Drosophila melanogaster and Saccharomyces cerevisiae was determined by stepwise degradation from the 3′-terminus and labelling with [3H]isoniazid. The sequence G-A-U-C-A-U-U-AOH was found at the 3′-terminus of both 18S rRNA species. Less extensive data for 18S RNA from a number of other eukaryotes are consistent with the same 3′-terminal sequence, and an identical sequence has previously been reported for the 3′-end of rabbit reticulocyte 18S rRNA (Hunt, 1970). These results suggest that the base sequence in this region is strongly conserved and may be identical in all eukaryotes. As the 3′-terminal hexanucleotide is complementary to eukaryotic terminator codons we discuss the possibility that the 3′-end of 18S rRNA may have a direct base-pairing role in the termination of protein synthesis.

scholarly journals ABERRANT INTRANUCLEOLAR MATURATION OF RIBOSOMAL PRECURSORS IN THE ABSENCE OF PROTEIN SYNTHESIS

1970 ◽  
Vol 45 (3) ◽  
pp. 554-564 ◽  
Author(s):  
Nessly C. Craig ◽  
Robert P. Perry
Keyword(s):  
Protein Synthesis ◽  
Ionic Strength ◽  
Ribosomal Rna ◽  
Buoyant Density ◽  
Protein Composition ◽  
28S Rrna ◽  
Maturation Process ◽  
Variable Response ◽  
Protein Complement

To help elucidate the role of protein in the maturation of ribosomal RNA in cultured L cells, we have studied the effects of cycloheximide upon the maturation process and upon the intranucleolar ribonucleoprotein particles containing the "preribosomal RNA's." Five parameters of these particles were analyzed: (a) extractability, (b) sedimentation characteristics in sucrose gradients, (c) RNA composition, (d) buoyant density in CsCl gradients, and (e) effects of increased ionic strength on the buoyant density. When protein synthesis is inhibited, the rate of conversion of the precursor 45S ribosomal RNA is rapidly diminished, falling to less than 30% of the control rate within 1 hr. Nevertheless, in terms of the first three parameters there is no difference between control and cycloheximide nucleolar particles. However, the cycloheximide particles have a lower and more heterogeneous buoyant density and a more variable response to increased ionic strength. The results imply that the protein composition of the cycloheximide particles is different from that of particles from control cells, and that the entire protein complement is not necessary for the first cleavages in the maturation process, although it is necessary for the normal rate of processing and for the eventual appearance of both 18S and 28S rRNA in mature ribosomes.

scholarly journals Role of 16S ribosomal RNA methylations in translation initiation in Escherichia coli

2008 ◽  
Vol 27 (6) ◽  
pp. 840-851 ◽  
Author(s):  
Gautam Das ◽  
Dinesh Kumar Thotala ◽  
Suman Kapoor ◽  
Sheelarani Karunanithi ◽  
Suman S Thakur ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Ribosomal Rna ◽  
Translation Initiation ◽  
16S Ribosomal Rna

The functional role of ribosomal RNA in protein synthesis

Cell ◽  
1989 ◽  
Vol 57 (4) ◽  
pp. 525-529 ◽  
Author(s):  
Albert E. Dahlberg
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Rna ◽  
Functional Role

Effect of point mutations in the decoding site (C1400) region of 16S ribosomal RNA on the ability of ribosomes to carry out individual steps of protein synthesis

Biochemistry ◽  
1989 ◽  
Vol 28 (3) ◽  
pp. 1012-1019 ◽  
Author(s):  
Robert Denman ◽  
Didier Negre ◽  
Philip R. Cunningham ◽  
Kelvin Nurse ◽  
John Colgan ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Rna ◽  
Point Mutations ◽  
16S Ribosomal Rna

Highly Conserved Base A55 of 16S Ribosomal RNA Is Important for the Elongation Cycle of Protein Synthesis

Biochemistry ◽  
2013 ◽  
Vol 52 (38) ◽  
pp. 6695-6701 ◽  
Author(s):  
Bhubanananda Sahu ◽  
Prashant K. Khade ◽  
Simpson Joseph
Keyword(s):  
Protein Synthesis ◽  
Ribosomal Rna ◽  
16S Ribosomal Rna ◽  
Elongation Cycle
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