Sequence comparison of glyceraldehyde-3-phosphate dehydrogenases from the three urkingdoms: evolutionary implication

1989 ◽  
Vol 35 (1) ◽  
pp. 81-85 ◽  
Author(s):  
Reinhard Hensel ◽  
Peter Zwickl ◽  
Stefan Fabry ◽  
Jutta Lang ◽  
Peter Palm
Keyword(s):  
Gene Transfer ◽  
Protein Evolution ◽  
Primary Structure ◽  
Ribonucleic Acid ◽  
Sequence Comparison ◽  
Structural Similarity ◽  
Evolutionary Implication ◽  
Ribosomal Ribonucleic Acid ◽  
Striking Deviation ◽  
Relationship Of

The primary structure of the glyceraldehyde-3-phosphate dehydrogenase from the archaebacteria shows striking deviation from the known sequences of eubacterial and eukaryotic sequences, despite unequivocal homologies in functionally important regions. Thus, the structural similarity between the eubacterial and eukaryotic enzymes is significantly higher than that between the archaebacterial enzymes and the eubacterial and eukarytic enzymes. This preferred similarity of eubacterial and eukaryotic glyceraldehyde-3-phosphate dehydrogenase structures does not correspond to the phylogenetic distances among the three urkingdoms as deduced from comparisons of ribosomal ribonucleic acid sequences. Indications will be presented that the closer relationship of the eubacterial and eukaryotic glyceraldehyde-3-phosphate dehydrogenase resulted from a gene transfer from eubacteria to eukaryotes after the segregation of the three urkingdoms.Key words: glyceraldehyde-3-phosphate dehydrogenase, archaebacteria, protein evolution.

scholarly journals Characterization of the binding of rat liver ribosomal proteins L6, L8, L19, S9, and S13 to 5.8 S ribosomal ribonucleic acid.

1981 ◽  
Vol 256 (14) ◽  
pp. 7207-7212
Author(s):  
K. Todokoro ◽  
N. Ulbrich ◽  
Y.L. Chan ◽  
I.G. Wool
Keyword(s):  
Rat Liver ◽  
Ribonucleic Acid ◽  
Ribosomal Proteins ◽  
Ribosomal Ribonucleic Acid

scholarly journals Nucleotide sequence of 5 S ribosomal ribonucleic acid of Iguana iguana.

1976 ◽  
Vol 251 (20) ◽  
pp. 6352-6354
Author(s):  
K L Roy ◽  
L Enns
Keyword(s):  
Nucleotide Sequence ◽  
Ribonucleic Acid ◽  
Iguana Iguana ◽  
Ribosomal Ribonucleic Acid

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.

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