Disease relevance of RPL7

• Characteristic epitope recognition pattern of autoantibodies against eukaryotic ribosomal protein L7 in systemic autoimmune diseases [1].
• The uptake into isolated HeLa nuclei of radioactive cytosol proteins and purified Escherichia coli ribosomal protein L7 is stimulated up to 4-fold by pancreatic deoxyribonuclease (DNase I) [2].
• Brucella ribosomal protein L7/L12 is a major component in the antigenicity of brucellin INRA for delayed-type hypersensitivity in brucella-sensitized guinea pigs [3].
• The immunogenic B. abortus ribosomal protein L7/L12 is a promising candidate antigen for the development of oral live vaccines against brucellosis, using food-grade lactic acid bacteria (LAB) as a carrier [4].
• The rplL gene, coding for ribosomal protein L7/L12 of Neisseria meningitidis was cloned and expressed as a fusion protein [5].

High impact information on RPL7

• Here we report that isolated ribosomal protein L7/12 strongly stimulates GTP hydrolysis by EF-G, but not by EF-Tu, indicating a major contribution of L7/12 to GTPase activation of EF-G on the ribosome [6].
• Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/12 [6].
• Human ribosomal protein L7 inhibits cell-free translation in reticulocyte lysates and affects the expression of nuclear proteins upon stable transfection into Jurkat T-lymphoma cells [7].
• By subtractive screening of a library made from mRNA of lipopolysaccharide (LPS)-stimulated mouse B lymphocytes we isolated cDNA-clones encoding the ribosomal protein L7 [8].
• The predicted amino acid sequence reveals that yeast YL8 is a homolog of mammalian ribosomal protein L7, E.coli L30 and others [9].

Chemical compound and disease context of RPL7

• An Escherichia coli mutant, LL103, harboring a mutation (Ser15 to Phe) in ribosomal protein L7/L12 was isolated among revertants of a streptomycin-dependent strain [10].

Biological context of RPL7

• We also showed that despite the fact that the 5' flanking region of the RPL7 sequence contains a potential TATA box upstream of an intact open reading frame, this pseudogene (RPL7P) is not actively transcribed [11].
• We demonstrated that the sequence is identical to the full-length RPL7 cDNA sequence, but lacks any recognizable introns, has a 30-bp poly(A) tail, and is bracketed by two perfect direct repeats of 14 bp [11].
• The RPL7 sequence was detected in a region of sequence overlapped by the cos2-e and cos1-22 cosmid clones but oriented opposite to the c-fms gene [11].
• During sequence analysis of the first intron of the human c-fms oncogene, we identified an open reading frame encoding the ribosomal protein L7 (RPL7) [11].
• Constitutive expression of human ribosomal protein L7 arrests the cell cycle in G1 and induces apoptosis in Jurkat T-lymphoma cells [12].

Anatomical context of RPL7

• Autoreactive human T cell lines recognizing ribosomal protein L7 [13].
• Recognition of rpL7 is HLA-DR6 restricted or respectively HLA-DP restricted in the two cell lines analyzed [13].
• In order to analyze the T cell response to rpL7 we cultured peripheral blood lymphocytes of healthy individuals and SLE patients in the presence of recombinant rpL7 [13].

Associations of RPL7 with chemical compounds

• The imidate compound was found to react with a high specificity with only one lysine residue of ribosomal protein L7/L12 [14].

Physical interactions of RPL7

• Human ribosomal protein L7 binds RNA with an alpha-helical arginine-rich and lysine-rich domain [15].

Other interactions of RPL7

• Rab11a, RPL7, and RPL28 showed moderate levels of differential expression [16].
• Three Methanocaldococcus jannaschii sRNP core proteins (ribosomal protein L7, Nop56/58, and fibrillarin) bind the box C/D sRNAs to assemble the sRNP complex, and these core proteins are essential for nucleotide methylation [17].
• The extent to which ribosomal protein L12 is acetylated to produce ribosomal protein L7 changes markedly with the growth rate [18].
• Ribosomal protein L7 has been established recently as a novel autoantigen representing a frequent target for autoantibodies from patients with systemic autoimmune diseases [19].
• Subsequent DNA sequence analysis identified these to be lysyl tRNA synthetase, ribosomal protein L7, ribosomal protein L9, beta transducin and TANK [20].

References