60S ribosomal protein L22

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Available structures
PDB Ortholog search: PDBe RCSB
Aliases RPL22, EAP, HBP15, HBP15/L22, L22, ribosomal protein L22
External IDs MGI: 99262 HomoloGene: 37378 GeneCards: RPL22
RNA expression pattern
PBB GE RPL22 208768 x at fs.png

PBB GE RPL22 220960 x at fs.png

PBB GE RPL22 214042 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 1: 6.18 – 6.21 Mb Chr 4: 152.33 – 152.33 Mb
PubMed search [1] [2]
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60S ribosomal protein L22 is a protein that in humans is encoded by the RPL22 gene on Chromosome 1.[3][4]


Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a cytoplasmic ribosomal protein that is a component of the 60S subunit. The protein belongs to the L22E family of ribosomal proteins. Its initiating methionine residue is post-translationally removed. The protein can bind specifically to Epstein–Barr virus-encoded small RNAs (EBERs) 1 and 2. The mouse protein has been shown to be capable of binding to heparin. Transcript variants utilizing alternative polyA signals exist. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. It was previously thought that this gene mapped to 3q26 and that it was fused to the acute myeloid leukemia 1 (AML1) gene located at 21q22 in some therapy-related myelodysplastic syndrome patients with 3;21 translocations; however, these fusions actually involve a ribosomal protein L22 pseudogene located at 3q26, and this gene actually maps to 1p36.3-p36.2.[4]

Together with RPL4, RPL22 forms the narrowest constriction of the ribosomal exit tunnel (the grove through which a growing protein chain exits the ribosome), and consequently mutations in RPL22 are believed to alter the efficiency with which protein synthesis proceeds.[5]


The gene may play a role in Insect toxicity resistance. In culex mosquitos, it was one of several ribosomal proteins which were overexpressed in strains resistant to the insecticide deltamethrin.[6] More focused analysis revealed that resistant mosquitoes expressed RPL22 at a level more than 2.5x higher than susceptible strains; however, the same study found that over-expression of RPL22 in transfected cells caused a down-regulation of a different deltamethrin-resistance gene (CYP6A1) and made these cells overall less resistant to the insecticide.[7] Less ambiguously, multiple studies indicate that mutations in RPL22 confer erythromycin resistance on E. coli bacteria.[8][9]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Nucifora G, Begy CR, Erickson P, Drabkin HA, Rowley JD (August 1993). "The 3;21 translocation in myelodysplasia results in a fusion transcript between the AML1 gene and the gene for EAP, a highly conserved protein associated with the Epstein-Barr virus small RNA EBER 1". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7784–8. doi:10.1073/pnas.90.16.7784. PMC 47227Freely accessible. PMID 8395054. 
  4. ^ a b "Entrez Gene: RPL22 ribosomal protein L22". 
  5. ^ Nakatogawa H, Ito K (2002). "The ribosomal exit tunnel functions as a discriminating gate". Cell. 108 (5): 629–36. doi:10.1016/S0092-8674(02)00649-9. PMID 11893334. 
  6. ^ Wu H, Tian H, Wu G, Langdon G, Kurtis J, Shen B, Ma L, Li X, Gu Y, Hu X, Zhu C (July 2004). "Culex pipiens pallens: identification of genes differentially expressed in deltamethrin-resistant and -susceptible strains". Pesticide Biochemistry and Physiology. 79 (3): 75–83. doi:10.1016/j.pestbp.2004.04.004. 
  7. ^ He J, Sun H, Zhang D, Sun Y, Ma L, Chen L, Liu Z, Xiong C, Yan G, Zhu C (June 2009). "Cloning and characterization of 60S ribosomal protein L22 (RPL22) from Culex pipiens pallens". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 153 (2): 216–22. doi:10.1016/j.cbpb.2009.03.003. PMID 19298862. 
  8. ^ Chittum HS, Champney WS (1994). "Ribosomal protein gene sequence changes in erythromycin-resistant mutants of Escherichia coli". Journal of Bacteriology. 176 (20): 6192–8. PMC 196958Freely accessible. PMID 7928988. 
  9. ^ Gabashvili IS, Gregory ST, Valle M, Grassucci R, Worbs M, Wahl MC, Dahlberg AE, Frank J (2001). "The polypeptide tunnel system in the ribosome and its gating in erythromycin resistance mutants of L4 and L22". Molecular Cell. 8 (1): 181–8. doi:10.1016/S1097-2765(01)00293-3. PMID 11511371. 

Further reading[edit]