The primary structure of rat ribosomal protein S24

Abstract

The amino acid sequence of rat ribosomal protein S24 was deduced from the sequence of nucieotides in a recombinant cDNA. 524 contains 133 amino acids and has a molecular mass of 15 413. Hybridi~tion of the cDNA to digests of nuclear DNA suggests that there are 12-16 copies of the S24 gene. The mRNA for the protein is about 600 nuckotides in length. Rat S24 is homologous to Xenopus iaevis S19 and related to Hal&c-terium morismortui ribosomal protein S15.Ribosomal protein S24; Amino acid sequence; cDNA; (Rat)

Characterization of the Human Small‐Ribosomal‐Subunit Proteins by N‐Terminal and Internal Sequencing, and Mass Spectrometry

“…Taking into account the accuracy of our measurements (10.1 -0.2% deviation from the masses of the proteins under investigation), the observed post-translational modifications of 4 0 s rp may be classified into several groups: proteins whose Nterminal methionine is removed in the native protein; this is the case for the human proteins S3a, S4, S9, S13, S14, S17, S19, S23, S26, S27, S29 and ,530; proteins which were found Nterminally blocked and whose N-terminal methionine should be removed because the masses fit to the sequence from the second amino acid residue of the deduced sequence; this is the case for proteins S11, S l 8 , S20 and S2. However, the mass deficit pointing to methionine removal may also be due to internal modification(s); in case of human protein S15, the N-terminal methionine was found blocked by acetylation as described for human S24 [36] ; proteins with unblocked N-termini but with modified internal amino acid residues; phosphorylation at serine as described for rat S6 [lo] was also found in human proteins S6 and S8; proteins with another type of blocking group at the N-terminus or at the side chain of an internal amino acid; this was observed for proteins S12 and S21.…”

“…P16632, PIR accession no. JH0213) and rat [36] (PIR accession no. S09197) rp available from the literature.…”

“…S24c mRNA represents the major form in undifferentiated and transformed cells, whereas the level of S24a mRNA is higher in differentiated cells [38]. Human [37] and rat [36] amino acid sequences of S24 were deduced from the nucleotide sequence of cDNAs which had been isolated from human fibrosarcoma or regenerating rat liver cDNA libraries. In our case the protein was directly isolated from human placenta, namely from differentiated cells which are not in the process of dividing.…”

Non-coordinate regulation of 5S rRNA genes and the gene encoding the 5S rRNA-binding ribosomal protein homolog in Neurospora crassa

“…Primers for ampli®cation of crp-4 sequences were based on two regions that are highly conserved in the yeast rpL5 (Tang and Nazar 1991) and rat L5 r-protein sequences (Chan et al 1987). The ampli®ed fragment was used to isolate two cDNA clones from a mycelial cDNA library.…”

Cdna Cloning, Characterization And Expression Analysis of Ribosomal Protein S24 Gene of Periplaneta Americana (Blattodea: Blattidae)

“…Although it may be unsufficient, the accumulation of these data are necessary for a solution of the structure of the organelle (Chan et al, 1990). Meanwhile, the information may also help to unravel the function of this protein, to understand the evolution of ribosomes, to define the rules that control the interaction of the proteins and rRNAs, and to reveal the amino acid sequences that direct the proteins to the nucleolus for assembly on nascent rRNA.…”