Purification, properties, and N-terminal amino acid sequence of certain 50S ribosomal subunit proteins from the archaebacterium Halobacterium cutirubrum.
Sixteen ribosomal proteins (r-proteins) from the 50S ribosomal subunit of the archaebacterium Halobacterium cutirubrum have been purified and their amino acid composition and partial N-terminal amino acid sequence have been determined. These proteins as a group are much more acidic than the large subunit r-proteins from eubacteria or eukaryotes. Little sequence homology is evident between the 50S subunit archaebacterial r-proteins and the equivalent proteins from the eubacterium Escherichia coli.
D000595:Amino Acid Sequence; D001665:Binding Sites; D006217:Halobacterium / Q000032:analysis*; D012335:RNA, Ribosomal / Q000378:metabolism; D012269:Ribosomal Proteins / Q000302:isolation & purification*; D012270:Ribosomes / Q000648:ultrastructure*
D012335:RNA, Ribosomal; D012269:Ribosomal Proteins