Amino acid sequence of the ribosomal protein HS23 from the halophilic Haloarcula marismortui and homology studies to other ribosomal proteins.
The ribosomal protein HS23 from the 30S subunit of the extreme halophilic Haloarcula marismortui, belonging to the group of archaea, was isolated either by RP-HLPLC or two-dimensional polyacrylamide gel electrophoresis. The complete amino acid sequence was determined by automated N-terminal microsequencing. The protein consists of 123 residues with a corresponding molecular mass of 12,552 Da as determined by electrospray mass spectroscopy; the pI is 11.04. Homology studies reveal similarities to the eukaryotic ribosomal protein S8 from Homo sapiens, Rattus norvegicus, Leishmania major, and Saccharomyces cerevisiae.
Engemann
S
S
Max-Delbrück-Centrum für Molekulare Medizin, Abteilung Proteinchemie, Berlin, Germany.
Herfurth
E
E
Briesemeister
U
U
Wittmann-Liebold
B
B
D000595:Amino Acid Sequence; D000818:Animals; D019843:Archaeal Proteins; D006217:Halobacterium / Q000737:chemistry*; D006801:Humans; D018320:Leishmania major / Q000737:chemistry; D008969:Molecular Sequence Data; D051381:Rats; D012269:Ribosomal Proteins / Q000737:chemistry*; D012441:Saccharomyces cerevisiae / Q000737:chemistry; D017385:Sequence Homology
D019843:Archaeal Proteins; D012269:Ribosomal Proteins; C095497:ribosomal protein HS23, Haloarcula marismortui