title: Sequence homologies in the N-terminal region of the ribosomal 'A' proteins from Methanobacterium Thermoautotrophicum and Halobacterium cutirubrum.
abstract: The ribosomal 'A' protein from the methanogen, Methanobacterium thermoautotrophicum, has been isolated and purified. The amino acid composition and mobility on two-dimensional gels indicates that this protein shows characteristics similar to the equivalent protein from the extreme halophile, Halobacterium cutirubrum, and is significantly different from the equivalent protein from other bacteria. The first 48 residues of the methanogenic 'A' protein were sequenced and showed a large amount of sequence homology to the H. cutirubrum 'A' protein. When the sequences of these two proteins were compared to the 'A' protein from other procaryotes (eubacteria), much less homology was evident. These results support the hypothesis (Woese, C.R. and Fox, G.F., (1977) Proc. Natl. Acad. Sci. U.S.A. 74, 5088-5090) of two procaryotic lines of evolutionary descent, the eubacteria and the archaebacteria, the latter including the methanogens and the extreme halophiles. The sequence data from the 'A' proteins also indicate that, phylogenetically, the archaebacteria are much closer to the cytoplasmic components of eucaryotes than they are to the eubacteria (or 'true bacteria').
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D004926:Escherichia coli / Q000032:analysis; D019605:Euryarchaeota / Q000032:analysis*; D006217:Halobacterium / Q000032:analysis*; D010944:Plants / Q000032:analysis; D012269:Ribosomal Proteins / Q000302:isolation & purification; D013045:Species Specificity; D014908:Triticum / Q000032:analysis
chemical_list: D012269:Ribosomal Proteins