The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

RPL11A  -  ribosomal 60S subunit protein L11A

Saccharomyces cerevisiae S288c

Synonyms: 60S ribosomal protein L11-A, L16, P8283.14, RP39, RP39A, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of RPL11A

  • Antibodies raised against a trpE-L16 fusion protein expressed in Escherichia coli were used to examine immunological relatedness between Saccharomyces cerevisiae ribosomal protein L16 and ribosomal proteins from eubacteria, halobacteria, methanogens, eocytes, and other eukaryotes [1].
  • The comparison of their sequences with those of ribosomal proteins from other organisms revealed that L23 and L33 are related to eubacterial ribosomal proteins from Escherichia coli and Bacillus stearothermophilus, while protein L16 was found to be homologous to a eukaryotic ribosomal protein from yeast [2].

High impact information on RPL11A


Biological context of RPL11A

  • The RPL16A-lacZ gene fusion partially complemented the slow growth or lethality of mutants containing null alleles of one or both RPL16 genes, respectively [1].
  • The predicted L16-like polypeptide is basic (pl 11.12), contains 232 amino acids (26.52 kDa) and has 36% amino acid sequence identity to E. coli L16 [7].
  • Immunoblot analysis with polyclonal antibodies to the L16-like polypeptide showed specific cross-reaction with a 22,000 Mr mitochondrial polypeptide that co-sediments with the large subunit of the mitochondrial ribosome in sucrose density gradients [7].
  • An open reading frame encoding a member of the L16 family of ribosomal proteins is adjacent to the URA7 gene on the left arm of chromosome II in Saccharomyces cerevisiae [7].
  • Because C1-3A sequences are bound in vitro by the transcription factor RAP1, the UAS activity of yeast telomere sequences was compared with that of a similar UAS from the tightly regulated ribosomal protein gene RP39A, which also contains a RAP1 binding site [8].

Anatomical context of RPL11A

  • Excess cry1 or RPL16 mRNA accumulated in polyribosomes in these cells and was translated at wild-type rates into rp59 or L16 proteins [3].

Associations of RPL11A with chemical compounds

  • An orthogonal experimental design L16 was used to investigate the effects of methanol, a gas mixture, zero air, temperature, agitation, and salts solution on hydrocarbon utilizing P. angusta [9].

Other interactions of RPL11A

  • We identified duplicated genes encoding ribosomal protein L11, RPL11B as a wild-type allele complementing the rrs2 mutation, and RPL11A in two-hybrid screening using RRS1 as bait [10].

Analytical, diagnostic and therapeutic context of RPL11A

  • Localization of Saccharomyces cerevisiae ribosomal protein L16 on the surface of 60 S ribosomal subunits by immunoelectron microscopy [1].
  • The following results were obtained: (1) The basic proteins L2, L16 and L33 and S20 bound f[3H]Met-tRNA to a similar extent as the total proteins from 30 S (TP30) or 50 S (TP50) when tested by nitrocellulose filtration, in contrast to the more acidic proteins L7/L12 and S8 [11].


  1. Localization of Saccharomyces cerevisiae ribosomal protein L16 on the surface of 60 S ribosomal subunits by immunoelectron microscopy. Tsay, Y.F., Shankweiler, G., Lake, J., Woolford, J.L. J. Biol. Chem. (1994) [Pubmed]
  2. The primary structures of ribosomal proteins L16, L23 and L33 from the archaebacterium Halobacterium marismortui. Hatakeyama, T., Hatakeyama, T., Kimura, M. FEBS Lett. (1988) [Pubmed]
  3. Ribosomal protein synthesis is not regulated at the translational level in Saccharomyces cerevisiae: balanced accumulation of ribosomal proteins L16 and rp59 is mediated by turnover of excess protein. Tsay, Y.F., Thompson, J.R., Rotenberg, M.O., Larkin, J.C., Woolford, J.L. Genes Dev. (1988) [Pubmed]
  4. Depletion of Saccharomyces cerevisiae ribosomal protein L16 causes a decrease in 60S ribosomal subunits and formation of half-mer polyribosomes. Rotenberg, M.O., Moritz, M., Woolford, J.L. Genes Dev. (1988) [Pubmed]
  5. Depletion of yeast ribosomal proteins L16 or rp59 disrupts ribosome assembly. Moritz, M., Paulovich, A.G., Tsay, Y.F., Woolford, J.L. J. Cell Biol. (1990) [Pubmed]
  6. Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16. Moritz, M., Pulaski, B.A., Woolford, J.L. Mol. Cell. Biol. (1991) [Pubmed]
  7. Identification of the yeast nuclear gene for the mitochondrial homologue of bacterial ribosomal protein L16. Pan, C., Mason, T.L. Nucleic Acids Res. (1995) [Pubmed]
  8. Properties of the transcriptional enhancer in Saccharomyces cerevisiae telomeres. Runge, K.W., Zakian, V.A. Nucleic Acids Res. (1990) [Pubmed]
  9. Effect of hydrocarbons and other parameters on hydrocarbon-utilizing Pichia angusta MTCC-225. Rao, R.S., Rasheed, M.A., Kalpana, G., Patil, D.J., Kumar, B. Appl. Biochem. Biotechnol. (2005) [Pubmed]
  10. Normal assembly of 60 S ribosomal subunits is required for the signaling in response to a secretory defect in Saccharomyces cerevisiae. Miyoshi, K., Tsujii, R., Yoshida, H., Maki, Y., Wada, A., Matsui, Y., Toh-E, A., Mizuta, K. J. Biol. Chem. (2002) [Pubmed]
  11. The complex between ribosomal proteins and aminoacyl-tRNA: the interactions and hydrolytic activities are not confined to the proteins L2 and L16 of Escherichia coli ribosomes. Sumpter, V.G., Tate, W.P., Nierhaus, K.H. Biochim. Biophys. Acta (1990) [Pubmed]
WikiGenes - Universities