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

RpL22  -  Ribosomal protein L22

Drosophila melanogaster

Synonyms: 60S ribosomal protein L22, CG7434, Dmel\CG7434, EG:BACR19J1.4, L22, ...
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.

High impact information on RpL22

  • Overexpression of either histone H1 or ribosomal protein L22 in Drosophila cells resulted in global suppression of the same set of genes, while depletion of H1 and L22 caused up-regulation of tested genes, suggesting that H1 and ribosomal proteins are essential for transcriptional gene repression [1].
  • GSCs express variant isoforms of general transcriptional components, translation initiation factors, and several variant ribosomal proteins, including RpL22, a protein enriched in several mammalian stem cells [2].
  • The predicted amino acid sequences from 109 to 269 of PBP-3 and from 184 to 312 of PBP-12 had more than 62% identities to mammalian L23a (rpl23a) and L22 (rpl22), the ribosomal proteins of the large subunit [3].
  • Expression analysis showed that, both during X. laevis embryogenesis and in X. laevis cultured cells during growth-rate changes, L22 synthesis is translationally regulated [4].
  • Using the yeast two-hybrid screening method, we found that the catalytic subunit of Drosophila melanogaster CKII (DmCKII) interacts with Drosophila ribosomal protein L22 (rpL22) [5].

Biological context of RpL22


Anatomical context of RpL22

  • Thus, Drosophila L22 and L23a might have two functions, namely the role of DNA-binding similar to histone H1 and the role of organizing the ribosome [3].

Associations of RpL22 with chemical compounds

  • The predicted full-length Drosophila rpL22 protein has an N-terminal extension rich in alanine, lysine, and proline that appears to be unique to Drosophila [5].

Other interactions of RpL22

  • From six independent cDNA clones isolated, we characterized two clones, PBP-3 and PBP-12 [3].


  1. Drosophila ribosomal proteins are associated with linker histone H1 and suppress gene transcription. Ni, J.Q., Liu, L.P., Hess, D., Rietdorf, J., Sun, F.L. Genes Dev. (2006) [Pubmed]
  2. The expression profile of purified Drosophila germline stem cells. Kai, T., Williams, D., Spradling, A.C. Dev. Biol. (2005) [Pubmed]
  3. Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and l23a, with unique histone-like amino-terminal extensions. Koyama, Y., Katagiri, S., Hanai, S., Uchida, K., Miwa, M. Gene (1999) [Pubmed]
  4. Xenopus laevis ribosomal protein L22: full-length cDNA sequence and expression analysis. Rapanotti, M.C., Pucci, B., Amaldi, F., Loreni, F. Gene (1995) [Pubmed]
  5. Interaction of casein kinase II with ribosomal protein L22 of Drosophila melanogaster. Zhao, W., Bidwai, A.P., Glover, C.V. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  6. Isolation of germline cells from Drosophila embryos by flow cytometry. Shigenobu, S., Arita, K., Kitadate, Y., Noda, C., Kobayashi, S. Dev. Growth Differ. (2006) [Pubmed]
WikiGenes - Universities