Disease relevance of RPL5

• Interaction of the HIV-1 rev cofactor eukaryotic initiation factor 5A with ribosomal protein L5 [1].
• The crystal structure of the ribosomal protein L5 from Bacillus stearothermophilus has been determined at 1.8 A resolution [2].

High impact information on RPL5

• The protein moiety of the 5S RNP has been identified as ribosomal protein L5, which is known to be released from ribosomes in a complex with 5S after various treatments of the 60S subunit [3].
• Here we show that the ribosomal protein L5, which is the central protein component of the 5S rRNA export system, is a cellular interaction partner of eIF-5A [1].
• Nucleophosmin is essential for ribosomal protein L5 nuclear export [4].
• Consistent with NPM's proposed role in ribosome biogenesis, we isolated ribosomal protein L5 (rpL5), a known chaperone for the 5S rRNA [4].
• Ribosomal protein L5 is part of the 60 S ribosomal subunit and localizes in both the cytoplasm and the nucleus of eukaryotic cells, accumulating particularly in the nucleoli [5].

Biological context of RPL5

• Cytosolic import factor- and Ran-independent nuclear transport of ribosomal protein L5 [6].
• Phosphorylation of ribosomal protein L5 by protein kinase CKII decreases its 5S rRNA binding activity [7].
• The rpl5 ribosomal protein gene was identified in the mitochondrial genome of the higher plant Oenothera berteriana [8].
• Eight of the nine C to U conversions in the rpl5 reading frame are non-silent and change the deduced amino acid sequence [8].
• The genes of the prokaryotic-like cistron that includes the rpsl9, rps3, rpl16, rpl5, and rpsl4 genes, which is at least partially conserved in the mitochondrial genomes of other higher and lower plants, are dispersed in the Oenothera mitochondrial genome [8].

Anatomical context of RPL5

• Ribosomal protein L5 is a shuttling protein that, in Xenopus oocytes, is involved in the nucleocytoplasmic transport of 5S rRNA [6].
• Transfer of RPS14 and RPL5 from the mitochondrion to the nucleus in grasses [9].

Associations of RPL5 with chemical compounds

• Subtractive suppressive hybridisation revealed overexpression of the ribosomal protein L5 in the doxorubicin resistant line [10].

Other interactions of RPL5

• Interaction of the beta subunit of casein kinase II with the ribosomal protein L5 [11].
• To better understand the strategies developed by higher plants to transfer organellar genes during evolution, we investigated the fate of the mitochondrial RPL5-RPS14 locus in grasses [9].
• This nuclear wheat RPL5 acquired its targeting information by duplication of an existing targeting presequence for another mitochondrial protein, ribosomal protein L4 [9].

Analytical, diagnostic and therapeutic context of RPL5

• Northern blot analysis of RNA prepared from the tRNA-Sepharose fraction showed the presence of 55SrRNA blot analysis of the tRNA-Sepharose fraction using an antibody against ribosomal protein L5, showed the presence of ribosomal protein L5 in this fraction [12].

References