Amino acid sequences of ribosomal proteins S11 from Bacillus stearothermophilus and S19 from Halobacterium marismortui Comparison of the ribosomal protein S11 family

Abstract

The complete amino acid sequences of ribosomal proteins Sl 1 from the Gram-positive eubacterium Bacillus sfearorhermophilus and of S19 from the archaebacterium Hulobocterium marismortui have been determined. A search for homologous sequences of these proteins revealed that they belong to the ribosomal protein Sl 1 family. Homologous proteins have previously been sequenced from Escherichia cofi as well as from chloroplast, yeast and mammalian ribosomes. A pairwise comparison of the amino acid sequences showed that Bacillus protein Sl 1 shares 68% identical residues with Sl 1 from Escherichiu coli and a slightly lower homology (52%) with the homologous chloroplast protein. The halophilic protein S19 is more related to the eukaryotic (45549%) than to the eubacterial counterparts (35%).

Impact of oxidative stress on the function, abundance, and turnover of the Arabidopsis 80S cytosolic ribosome

“…It should be noted that RPS14C was quite stable under control conditions so this increase did not make RSP14C a highly unstable protein under oxidative stress conditions compared to other r-proteins (Table 1). This protein is equivalent to the bacterial S11 rprotein family that has been shown to play an important role in selecting the correct tRNA in protein biosynthesis (Kimura et al, 1988). In yeast S14 is also required for production of stable ribosome assembly intermediates and mature ribosomes, with a particular function in late steps of 40S ribosomal subunit maturation and pre-rRNA processing (Jakovljevic et al, 2004).…”