OAS1
From Wikipedia, the free encyclopedia
An Error has occurred retrieving Wikidata item for infobox Template:Cs1 config 2'-5'-oligoadenylate synthetase 1 is an enzyme that in humans is encoded by the OAS1 gene.[1][2]
This gene encodes a member of the 2-5A synthetase family, which include essential proteins involved in the innate immune response to viral infection.
The encoded protein is induced by interferons and uses adenosine triphosphate in 2'-specific nucleotidyl transfer reactions to synthesize 2',5'-oligoadenylates (2-5As). These molecules activate latent RNase L, which results in both viral and endogenous RNA degradation and the inhibition of viral replication. The three known members of this gene family are located in a cluster on chromosome 12. Hypomorphic mutations in this gene have been associated with host susceptibility to viral infection, while gain-of-function variants can cause autoinflammatory immunodeficiency.[3] Alternatively spliced transcript variants encoding different isoforms have been described.[4]
References
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- ^ Page Module:Citation/CS1/styles.css has no content.Renault B, Hovnanian A, Bryce S, Chang JJ, Lau S, Sakuntabhai A, et al. (October 1997). "A sequence-ready physical map of a region of 12q24.1". Genomics. 45 (2): 271–278. doi:10.1006/geno.1997.4888. PMID 9344649.
- ^ Page Module:Citation/CS1/styles.css has no content.Nechiporuk T, Nechiporuk A, Sahba S, Figueroa K, Shibata H, Chen XN, et al. (September 1997). "A high-resolution PAC and BAC map of the SCA2 region". Genomics. 44 (3): 321–329. doi:10.1006/geno.1997.4886. PMID 9325053.
- ^ Page Module:Citation/CS1/styles.css has no content.Magg T, Okano T, Koenig LM, Boehmer DF, Schwartz SL, Inoue K, et al. (June 2021). "Heterozygous OAS1 gain-of-function variants cause an autoinflammatory immunodeficiency". Science Immunology. 6 (60) eabf9564. doi:10.1126/sciimmunol.abf9564. PMC 8392508. PMID 34145065.
- ^ Page Module:Citation/CS1/styles.css has no content."Entrez Gene: OAS1 2',5'-oligoadenylate synthetase 1, 40/46kDa".
Further reading
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- Page Module:Citation/CS1/styles.css has no content.Justesen J, Hartmann R, Kjeldgaard NO (October 2000). "Gene structure and function of the 2'-5'-oligoadenylate synthetase family". Cellular and Molecular Life Sciences. 57 (11): 1593–1612. doi:10.1007/PL00000644. PMC 11146851. PMID 11092454. S2CID 19154357.
- Page Module:Citation/CS1/styles.css has no content.Ghosh SK, Kusari J, Bandyopadhyay SK, Samanta H, Kumar R, Sen GC (August 1991). "Cloning, sequencing, and expression of two murine 2'-5'-oligoadenylate synthetases. Structure-function relationships". The Journal of Biological Chemistry. 266 (23): 15293–15299. doi:10.1016/S0021-9258(18)98615-1. PMID 1651324.
- Page Module:Citation/CS1/styles.css has no content.Silverman RH, Sengupta DN (1991). "Translational regulation by HIV leader RNA, TAT, and interferon-inducible enzymes". Journal of Experimental Pathology. 5 (2): 69–77. PMID 1708818.
- Page Module:Citation/CS1/styles.css has no content.Saunders ME, Gewert DR, Tugwell ME, McMahon M, Williams BR (July 1985). "Human 2-5A synthetase: characterization of a novel cDNA and corresponding gene structure". The EMBO Journal. 4 (7): 1761–1768. doi:10.1002/j.1460-2075.1985.tb03848.x. PMC 554415. PMID 2411547.
- Page Module:Citation/CS1/styles.css has no content.Benech P, Mory Y, Revel M, Chebath J (September 1985). "Structure of two forms of the interferon-induced (2'-5') oligo A synthetase of human cells based on cDNAs and gene sequences". The EMBO Journal. 4 (9): 2249–2256. doi:10.1002/j.1460-2075.1985.tb03922.x. PMC 554493. PMID 2416561.
- Page Module:Citation/CS1/styles.css has no content.Williams BR, Saunders ME, Willard HF (July 1986). "Interferon-regulated human 2-5A synthetase gene maps to chromosome 12". Somatic Cell and Molecular Genetics. 12 (4): 403–408. doi:10.1007/BF01570735. PMID 2426799. S2CID 13077134.
- Page Module:Citation/CS1/styles.css has no content.Hovanessian AG, Laurent AG, Chebath J, Galabru J, Robert N, Svab J (May 1987). "Identification of 69-kd and 100-kd forms of 2-5A synthetase in interferon-treated human cells by specific monoclonal antibodies". The EMBO Journal. 6 (5): 1273–1280. doi:10.1002/j.1460-2075.1987.tb02364.x. PMC 553929. PMID 2440675.
- Page Module:Citation/CS1/styles.css has no content.Rutherford MN, Hannigan GE, Williams BR (March 1988). "Interferon-induced binding of nuclear factors to promoter elements of the 2-5A synthetase gene". The EMBO Journal. 7 (3): 751–759. doi:10.1002/j.1460-2075.1988.tb02872.x. PMC 454386. PMID 2456211.
- Page Module:Citation/CS1/styles.css has no content.Benech P, Vigneron M, Peretz D, Revel M, Chebath J (December 1987). "Interferon-responsive regulatory elements in the promoter of the human 2',5'-oligo(A) synthetase gene". Molecular and Cellular Biology. 7 (12): 4498–4504. doi:10.1128/MCB.7.12.4498. PMC 368134. PMID 2830497.
- Page Module:Citation/CS1/styles.css has no content.Wathelet MG, Clauss IM, Nols CB, Content J, Huez GA (December 1987). "New inducers revealed by the promoter sequence analysis of two interferon-activated human genes". European Journal of Biochemistry. 169 (2): 313–321. doi:10.1111/j.1432-1033.1987.tb13614.x. PMID 3121313.
- Page Module:Citation/CS1/styles.css has no content.Wathelet MG, Szpirer J, Nols CB, Clauss IM, De Wit L, Islam MQ, et al. (September 1988). "Cloning and chromosomal location of human genes inducible by type I interferon". Somatic Cell and Molecular Genetics. 14 (5): 415–426. doi:10.1007/BF01534709. PMID 3175763. S2CID 42406993.
- Page Module:Citation/CS1/styles.css has no content.Wathelet M, Moutschen S, Cravador A, DeWit L, Defilippi P, Huez G, et al. (February 1986). "Full-length sequence and expression of the 42 kDa 2-5A synthetase induced by human interferon". FEBS Letters. 196 (1): 113–120. Bibcode:1986FEBSL.196..113W. doi:10.1016/0014-5793(86)80224-1. PMID 3753689. S2CID 38673605.
- Page Module:Citation/CS1/styles.css has no content.Shiojiri S, Fukunaga R, Ichii Y, Sokawa Y (May 1986). "Structure and expression of a cloned cDNA for human (2'-5')oligoadenylate synthetase". Journal of Biochemistry. 99 (5): 1455–1464. doi:10.1093/oxfordjournals.jbchem.a135615. PMID 3754863.
- Page Module:Citation/CS1/styles.css has no content.Merlin G, Chebath J, Benech P, Metz R, Revel M (August 1983). "Molecular cloning and sequence of partial cDNA for interferon-induced (2'-5')oligo(A) synthetase mRNA from human cells". Proceedings of the National Academy of Sciences of the United States of America. 80 (16): 4904–4908. Bibcode:1983PNAS...80.4904M. doi:10.1073/pnas.80.16.4904. PMC 384155. PMID 6348777.
- Page Module:Citation/CS1/styles.css has no content.Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–174. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Page Module:Citation/CS1/styles.css has no content.Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–156. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Page Module:Citation/CS1/styles.css has no content.Ghosh A, Sarkar SN, Guo W, Bandyopadhyay S, Sen GC (December 1997). "Enzymatic activity of 2'-5'-oligoadenylate synthetase is impaired by specific mutations that affect oligomerization of the protein". The Journal of Biological Chemistry. 272 (52): 33220–33226. doi:10.1074/jbc.272.52.33220. PMID 9407111.
- Page Module:Citation/CS1/styles.css has no content.Hovnanian A, Rebouillat D, Mattei MG, Levy ER, Marié I, Monaco AP, et al. (September 1998). "The human 2',5'-oligoadenylate synthetase locus is composed of three distinct genes clustered on chromosome 12q24.2 encoding the 100-, 69-, and 40-kDa forms". Genomics. 52 (3): 267–277. doi:10.1006/geno.1998.5443. PMID 9790745.
- Page Module:Citation/CS1/styles.css has no content.Sarkar SN, Ghosh A, Wang HW, Sung SS, Sen GC (September 1999). "The nature of the catalytic domain of 2'-5'-oligoadenylate synthetases". The Journal of Biological Chemistry. 274 (36): 25535–25542. doi:10.1074/jbc.274.36.25535. PMID 10464285.
