Disease relevance of RPL5

• H. cutirubrum HL19, however, has structural identity with E. coli L5 and seems to be related to yeast YL3 and, hence, may be an evolutionary link between the prokaryotic and eukaryotic 5 S rRNA-binding proteins [1].
• A novel operon organization involving the genes for chorismate synthase (aromatic biosynthesis pathway) and ribosomal GTPase center proteins (L11, L1, L10, L12: rplKAJL) in cyanobacterium Synechocystis PCC 6803 [2].
• The quadrivalent HPV vaccine is a mixture of four HPV type-specific VLPs prepared from the L1 proteins of HPV 6, 11, 16, and 18 combined with an aluminum adjuvant [3].

High impact information on RPL5

• A conditional null mutant in which the only copy of RPL1 is under control of the repressible GAL1 promoter was constructed [4].
• Ribosomal protein L1 from Saccharomyces cerevisiae binds 5S rRNA and can be released from intact 60S ribosomal subunits as an L1-5S ribonucleoprotein (RNP) particle [4].
• The 5 S RNA binding protein (YL3) also appears not to influence directly the maturation process, but rather to play a role in protecting the rRNA from further degradation by "housekeeping" nucleases [5].
• To identify residues important for binding of Saccharomyces cerevisiae rpL1 to 5 S rRNA and assembly into functional ribosomes, we have isolated mutant alleles of the yeast RPL1 gene by site-directed and random mutagenesis [6].
• UPF1-3EP and L1 co-distributed with polyribosomes fractionated in a 7-47% sucrose gradient [7].

Biological context of RPL5

• A gene encoding the 5 S rRNA-binding protein (YL3) in yeast (Saccharomyces cerevisiae) was further characterized with respect to its chromosomal localization, the controlling sequence regions, and the influence of 5 S rRNA gene expression [8].
• A rice (Oryza sativa L.) cDNA encodes a protein sequence homologous to the eukaryotic ribosomal 5S RNA-binding protein [9].
• Mutant proteins containing single or multiple amino acid substitutions were generated by site-directed mutagenesis of the L1 gene carried on a plasmid [10].
• Effects of these mutations on cell viability and ribosome assembly were characterized by transformation of a conditional null L1 yeast mutant with the mutated L1 gene expressed from the plasmid [10].

Anatomical context of RPL5

• Multiple regions of yeast ribosomal protein L1 are important for its interaction with 5 S rRNA and assembly into ribosomes [6].
• Immunodepletion of the cell-free system with anti-YL3 IgG was found to increase the sensitivity of 5 S rRNA synthesis to inhibition by 5 S rRNA [11].
• When polyribosomes were disaggregated, UPF1-3EP and L1 accumulated in fractions coincident with 80S ribosomal particles [7].

Associations of RPL5 with chemical compounds

• This effect is accomplished by modification with phenylglyoxal of only 3 arginine residues per YL3 molecule [12].
• In contrast, a large number of protein YL3 amino groups must be modified by acetic anhydride to prevent complex formation [12].
• Involvement of lysine and arginine residues in the binding of yeast ribosomal protein YL3 to 5S RNA [12].
• Treatment of protein YL3 with acetic anhydride, maleic anhydride or phenylglyoxal is accompanied by loss of its capacity to bind to 5S RNA [12].
• The 5S rRNA-ribosomal protein YL3 ribonucleoprotein particle was isolated from yeast cells labeled with [32P]orthophosphate [13].

Physical interactions of RPL5

• A two-dimensional gel electrophoresis method was used to demonstrate assembly of newly synthesized 5 S rRNA into a ribonucleoprotein complex containing ribosomal protein YL3 [11].
• Contributions of the highly conserved K270 and its neighboring K271 in the C-terminal region of the yeast ribosomal protein L1 to 5S rRNA binding and ribosome assembly were examined by in vivo and in vitro studies on the consequences of 14 substitution mutations [14].

Other interactions of RPL5

• An L1-5S RNP particle not associated with ribosomal particles was detected by coimmunoprecipitation of L1 and 5S rRNA [4].
• We propose a model for the regulation of yeast 5 S rRNA synthesis in which YL3 competes with the presumptive transcription factor IIIA analog for binding of 5 S rRNA [11].

Analytical, diagnostic and therapeutic context of RPL5

• The complex comprising 5S ribosomal RNA and the ribosomal protein YL3 (5S rRNP) was isolated from yeast (Saccharomyces cerevisiae), and positively contrasted preparations were imaged by transmission electron microscopy [15].

References