HL35e and HLA: primary structure of two very basic and cysteine-rich ribosomal proteins from Haloarcula marismortui.
Two small and very basic ribosomal proteins have been purified from the 50S ribosomal subunit of the archaebacterium Haloarcula marismortui by RP-HPLC. The complete primary structures of these two proteins, which we refer to as HL35e and HLA, have been determined by protein chemical methods. Both proteins are characterized by a high content of basic amino acids and the presence of two pairs of cysteines in each polypeptide chain, one of which resembles the C4-zinc-finger motif. Comparison of the protein sequences with those of other ribosomal proteins revealed that HL35e shows significant sequence homology exclusively to eukaryotic ribosomal proteins, namely to yeast L35 and to L37 from rat. For HLA no homologous ribosomal protein so far known could be found. Obviously, HL35e and HLA have no counterparts in eubacterial ribosomes.
Bergmann
U
U
Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, Berlin, Germany.
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003545:Cysteine; D006216:Halobacteriaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D012269:Ribosomal Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid
D001426:Bacterial Proteins; C081462:RPL37E protein, Haloarcula marismortui; C081463:RPL44E protein, Haloarcula marismortui; D012269:Ribosomal Proteins; D003545:Cysteine