60S ribosomal protein L22

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RPL22
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRPL22, EAP, HBP15, HBP15/L22, L22, ribosomal protein L22
External IDsOMIM: 180474 MGI: 99262 HomoloGene: 37378 GeneCards: RPL22
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_000983

NM_001277113
NM_001277114
NM_009079

RefSeq (protein)

NP_000974

NP_001264042
NP_001264043
NP_033105

Location (UCSC)Chr 1: 6.19 – 6.21 MbChr 4: 152.41 – 152.42 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

60S ribosomal protein L22 is a protein that in humans is encoded by the RPL22 gene on Chromosome 1.[5][6]

Function

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 RNA (EBER) 1. 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.[6]

Insects

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.[7] 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.[8]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000116251 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028936 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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. Bibcode:1993PNAS...90.7784N. doi:10.1073/pnas.90.16.7784. PMC 47227. PMID 8395054.
  6. ^ a b "Entrez Gene: RPL22 ribosomal protein L22".
  7. ^ Wu HW, Tian HS, Wu GL, Langdon G, Kurtis J, Shen B, Ma L, Li XL, Gu Y, Hu XB, Zhu CL (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.
  8. ^ 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. S2CID 5058277.

Further reading

External links

  • Overview of all the structural information available in the PDB for UniProt: P35268 (60S ribosomal protein L22) at the PDBe-KB.