40S ribosomal protein S27 also known as metallopan-stimulin 1 or MPS-1 is a protein that in humans is encoded by the RPS27gene.[1][2][3] Metallopanstimulin is a zinc finger protein proposed to be involved DNA repair as well as oncogenesis.[4]
Ribosomes, the organelles that catalyzeprotein 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 ribosomal protein that is a component of the 40S subunit. The protein belongs to the S27E family of ribosomal proteins. It contains a C4-type zinc finger domain that can bind to zinc. The encoded protein has been shown to be able to bind to nucleic acid. It is located in the cytoplasm as a ribosomal component, but it has also been detected in the nucleus. Studies in rat indicate that ribosomal protein S27 is located near ribosomal protein S18 in the 40S subunit and is covalently linked to translation initiation factor eIF3. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[3]
Clinical significance
Its expression is increased in several types of malignancy and MPS levels have been reported to drop with treatment of some cancers. It has also been used as a target for some chemotherapies, which aim to chelate out the zinc from the zinc finger motif of the MPS, thus yielding it inactive. These therapies have shown promise for the treatment of cancer in laboratory experiments and some limited clinical trials. Head and neck cancer transfected to overexpress this protein have demonstrated suppressed growth.[4]
References
↑Tsui SK, Lee SM, Fung KP, Waye MM, Lee CY (Oct 1996). "Primary structures and sequence analysis of human ribosomal proteins L39 and S27". Biochemistry and Molecular Biology International. 40 (3): 611–6. doi:10.1080/15216549600201203. PMID8908372.
↑Fernandez-Pol JA, Klos DJ, Hamilton PD (Oct 1993). "A growth factor-inducible gene encodes a novel nuclear protein with zinc finger structure". The Journal of Biological Chemistry. 268 (28): 21198–204. PMID8407955.
↑ 4.04.1Fernandez-Pol JA (1996). "Metallopanstimulin as a novel tumor marker in sera of patients with various types of common cancers: implications for prevention and therapy". Anticancer Research. 16 (4B): 2177–85. PMID8694540.
Further reading
Scurry WC, Stack BC (Dec 2007). "Role of metalloproteins in the clinical management of head and neck squamous cell carcinoma". Head & Neck. 29 (12): 1144–55. doi:10.1002/hed.20655. PMID17657798.
Lee WJ, Keefer K, Hollenbeak CS, Stack BC (Oct 2004). "A new assay to screen for head and neck squamous cell carcinoma using the tumor marker metallopanstimulin". Otolaryngology–Head and Neck Surgery. 131 (4): 466–71. doi:10.1016/j.otohns.2004.03.011. PMID15467619.
Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochemistry and Cell Biology. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID8722009.
Fernandez-Pol JA, Klos DJ, Hamilton PD (Aug 1994). "Metallopanstimulin gene product produced in a baculovirus expression system is a nuclear phosphoprotein that binds to DNA". Cell Growth & Differentiation. 5 (8): 811–25. PMID7986747.
Vladimirov SN, Ivanov AV, Karpova GG, Musolyamov AK, Egorov TA, Thiede B, Wittmann-Liebold B, Otto A (Jul 1996). "Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry". European Journal of Biochemistry / FEBS. 239 (1): 144–9. doi:10.1111/j.1432-1033.1996.0144u.x. PMID8706699.
Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (May 1998). "A map of 75 human ribosomal protein genes". Genome Research. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID9582194.
Atsuta Y, Aoki N, Sato K, Oikawa K, Nochi H, Miyokawa N, Hirata S, Kimura S, Sasajima T, Katagiri M (Aug 2002). "Identification of metallopanstimulin-1 as a member of a tumor associated antigen in patients with breast cancer". Cancer Letters. 182 (1): 101–7. doi:10.1016/S0304-3835(02)00068-X. PMID12175529.
Martin-Lluesma S, Stucke VM, Nigg EA (Sep 2002). "Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2". Science. 297 (5590): 2267–70. doi:10.1126/science.1075596. PMID12351790.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
Bhonde MR, Hanski ML, Budczies J, Cao M, Gillissen B, Moorthy D, Simonetta F, Scherübl H, Truss M, Hagemeier C, Mewes HW, Daniel PT, Zeitz M, Hanski C (Mar 2006). "DNA damage-induced expression of p53 suppresses mitotic checkpoint kinase hMps1: the lack of this suppression in p53MUT cells contributes to apoptosis". The Journal of Biological Chemistry. 281 (13): 8675–85. doi:10.1074/jbc.M511333200. PMID16446370.
Wang YW, Qu Y, Li JF, Chen XH, Liu BY, Gu QL, Zhu ZG (Aug 2006). "In vitro and in vivo evidence of metallopanstimulin-1 in gastric cancer progression and tumorigenicity". Clinical Cancer Research. 12 (16): 4965–73. doi:10.1158/1078-0432.CCR-05-2316. PMID16914586.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID17081983.
