Amino acid sequence of the ribosomal protein HS23 from the halophilicHaloarcula marismortui and homology studies to other ribosomal proteins |
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Authors: | Sabine Engemann Elke Herfurth Ulrike Briesemeister and Brigitte Wittmann-Liebold |
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Institution: | (1) Abteilung Proteinchemie, Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Strasse 10, 13125 Berlin, Germany |
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Abstract: | The ribosomal protein HS23 from the 30S subunit of the extreme halophilicHaloarcula 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 fromHomo sapiens, Rattus norvegicus, Leishmania major, andSaccharomyces cerevisiae.Abbreviations
H. marismortui
Haloarcula marismortui
- PVDF
polyvinylidene difluoride
- PTH
phenylthiohydantoin
- RP-HPLC
reversed-phase high-performance liquid chromatography
- TFA
trifluoro acetic acid
- TP30
total protein mixture from the 30S ribosomal subunit ofH. marismortui |
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Keywords: | Ribosomal proteins protein sequencing evolution Haloarcula marismortui |
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