N-terminal modification and amino-acid sequence of the ribosomal protein HmaS7 from Haloarcula marismortui and homology studies to other ribosomal proteins. 1993

S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Berlin.

The ribosomal protein HmaS7 from the 30S subunit of the extreme halophilic archaeum Haloarcula marismortui was isolated by semi-preparative RP-HPLC. The complete amino-acid sequence of this protein was determined by automated microsequence analysis of appropriate peptide fragments from several proteinase digests. The entire protein consists of 205 amino acids with a corresponding molecular mass of 22580 Da. The modification at the amino-terminal amino acid was deblocked so that the N-terminal amino acids could be sequenced and the type of the modification was identified as an acetyl group by electrospray mass spectrometry of suitable peptides. Homology studies of HmaS7 showed similarities to ribosomal proteins derived from organisms of all three urkingdoms, such as to EcoS7, HmoS7, MvaS7, SacS7 and RatS7; due to the strong sequence homologies found within the archaebacterial ribosomal proteins we conclude that the protein sequence which was determined for S7 from Methanococcus vannielii by nucleotide sequencing of the gene should be about 20 or 30 amino acids longer than previously published (Lechner, K., Heller, G. & Böck, A. (1989) J. Mol. Evol. 29, 20-27).

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009626 Terminology as Topic Works about the terms, expressions, designations, or symbols used in a particular science, discipline, or specialized subject area. Etymology,Nomenclature as Topic,Etymologies
D002851 Chromatography, High Pressure Liquid Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed. Chromatography, High Performance Liquid,Chromatography, High Speed Liquid,Chromatography, Liquid, High Pressure,HPLC,High Performance Liquid Chromatography,High-Performance Liquid Chromatography,UPLC,Ultra Performance Liquid Chromatography,Chromatography, High-Performance Liquid,High-Performance Liquid Chromatographies,Liquid Chromatography, High-Performance
D004591 Electrophoresis, Polyacrylamide Gel Electrophoresis in which a polyacrylamide gel is used as the diffusion medium. Polyacrylamide Gel Electrophoresis,SDS-PAGE,Sodium Dodecyl Sulfate-PAGE,Gel Electrophoresis, Polyacrylamide,SDS PAGE,Sodium Dodecyl Sulfate PAGE,Sodium Dodecyl Sulfate-PAGEs
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001105 Archaea One of the three domains of life (the others being BACTERIA and Eukarya), formerly called Archaebacteria under the taxon Bacteria, but now considered separate and distinct. They are characterized by: (1) the presence of characteristic tRNAs and ribosomal RNAs; (2) the absence of peptidoglycan cell walls; (3) the presence of ether-linked lipids built from branched-chain subunits; and (4) their occurrence in unusual habitats. While archaea resemble bacteria in morphology and genomic organization, they resemble eukarya in their method of genomic replication. The domain contains at least four kingdoms: CRENARCHAEOTA; EURYARCHAEOTA; NANOARCHAEOTA; and KORARCHAEOTA. Archaebacteria,Archaeobacteria,Archaeon,Archebacteria
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012269 Ribosomal Proteins Proteins found in ribosomes. They are believed to have a catalytic function in reconstituting biologically active ribosomal subunits. Proteins, Ribosomal,Ribosomal Protein,Protein, Ribosomal
D012270 Ribosomes Multicomponent ribonucleoprotein structures found in the CYTOPLASM of all cells, and in MITOCHONDRIA, and PLASTIDS. They function in PROTEIN BIOSYNTHESIS via GENETIC TRANSLATION. Ribosome
D013058 Mass Spectrometry An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers. Mass Spectroscopy,Spectrometry, Mass,Spectroscopy, Mass,Spectrum Analysis, Mass,Analysis, Mass Spectrum,Mass Spectrum Analysis,Analyses, Mass Spectrum,Mass Spectrum Analyses,Spectrum Analyses, Mass

Related Publications

S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
May 1995, Journal of protein chemistry,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
August 1994, FEBS letters,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
August 1987, Biological chemistry Hoppe-Seyler,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
November 1995, European journal of biochemistry,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
December 1992, FEBS letters,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
December 1980, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
December 1979, Hoppe-Seyler's Zeitschrift fur physiologische Chemie,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
June 2013, Acta crystallographica. Section D, Biological crystallography,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
April 2002, Journal of molecular biology,
S Klussmann, and P Franke, and U Bergmann, and S Kostka, and B Wittmann-Liebold
August 1973, Canadian journal of biochemistry,
Copied contents to your clipboard!