Regulation of mitochondrial ribosomal protein S29 (MRPS29) expression by a 5′-upstream open reading frame

Mitochondrion

Volumn 10, Issue 3, 2010, Pages 274-283

  Han, Min Joon ^a   Chiu, Daniel T ^b   Koc, Emine C ^a  

^a PENNSYLVANIA STATE UNIVERSITY   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

Apoptosis; DAP3; Mitochondrial translation; Ribosome; UORF

Indexed keywords

MESSENGER RNA; MITOCHONDRIAL PROTEIN; RIBOSOME PROTEIN; RIBOSOME PROTEIN S29; UNCLASSIFIED DRUG;

5' UNTRANSLATED REGION; APOPTOSIS; ARTICLE; ATAXIA TELANGIECTASIA; CELL STRAIN HEK293; CELL STRAIN K 562; CONTROLLED STUDY; DNA FLANKING REGION; EXPRESSED SEQUENCE TAG; GENE EXPRESSION REGULATION; GENE OVEREXPRESSION; GLIOMA CELL; HELA CELL; HUMAN; HUMAN CELL; LEUKEMIA CELL LINE; MITOCHONDRION; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; REAL TIME POLYMERASE CHAIN REACTION; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RIBOSOME; SEQUENCE DATABASE;

5' UNTRANSLATED REGIONS; APOPTOSIS REGULATORY PROTEINS; CELL LINE; EXPRESSED SEQUENCE TAGS; GENE EXPRESSION REGULATION; HUMANS; OPEN READING FRAMES; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RIBOSOMAL PROTEINS;

ATAXIA TELANGIECTASIA;

EID: 77949916020     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2009.12.150     Document Type: Article

References (45)

1. Ame J.C., Spenlehauer C., de Murcia G. The PARP superfamily. Bioassays 2004, 26:882-893.
2. Au H.C., Scheffler I.E. A respiration-deficient Chinese hamster cell line with a defect in mitochondrial protein synthesis: rapid turnover of some mitochondrial transcripts. Somat. Cell Mol. Genet. 1997, 23:27-35.
3. Berger T., Brigl M., Herrmann J.M., Vielhauer V., Luckow B., Schlondorff D., Kretzler M. The apoptosis mediator mDAP-3 is a novel member of a conserved family of mitochondrial proteins. J. Cell Sci. 2000, 113:3603-3612.
4. Bo H., Ghazizadeh M., Shimizu H., Kurihara Y., Egawa S., Moriyama Y., Tajiri T., Kawanami O. Effect of ionizing irradiation on human esophageal cancer cell lines by cDNA microarray gene expression analysis. J. Nippon Med. Sch. 2004, 71:172-180.
5. Calvo S.E., Pagliarini D.J., Mootha V.K. Upstream open reading frames cause widespread reduction of protein expression and are polymorphic among humans. Proc. Natl. Acad. Sci. USA 2009, 106:7507-7512.
6. Chen Y., Cairns R., Papandreou I., Koong A., Denko N.C. Oxygen consumption can regulate the growth of tumors, a new perspective on the Warburg effect. PLoS One 2009, 4:e7033.
7. Chintharlapalli S.R., Jasti M., Malladi S., Parsa K.V., Ballestero R.P., Gonzalez-Garcia M. BMRP is a Bcl-2 binding protein that induces apoptosis. J. Cell Biochem. 2005, 94:611-626.
8. Danial N.N., Korsmeyer S.J. Cell death: critical control points. Cell 2004, 116:205-219.
9. Denslow N., Anders J., O'Brien T.W. Bovine mitochondrial ribosomes possess a high affinity binding site for guanine nucleotides. J. Biol. Chem. 1991, 266:9586-9590.
10. Hamilton M.G., O'Brien T.W. Ultracentrifugal characterization of the mitochondrial ribosome and subribosomal particles of bovine liver: molecular size and composition. Biochemistry 1974, 13:5400-5403.
11. Henning, K.A., 1993. The molecular genetics of human diseases with defective DNA damage. Stanford University.
12. Jacques C., Fontaine J.-F., Franc B., Mirebeau-Prunier D., Triau S., Savagner F., Malthiery Y. Death-associated protein 3 is overexpressed in human thyroid oncocytic tumours. Brit. J. Cancer 2009, 101:132-138.
13. Kim H.R., Chae H.J., Thomas M., Miyazaki T., Monosov A., Monosov E., Krajewska M., Krajewski S., Reed J.C. Mammalian dap3 is an essential gene required for mitochondrial homeostasis in vivo and contributing to the extrinsic pathway for apoptosis. FASEB J. 2007, 21:188-196.
14. Kissil J.L., Cohen O., Raveh T., Kimchi A. Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death. EMBO J. 1999, 18:353-362.
15. Kissil J.L., Deiss L.P., Bayewitch M., Raveh T., Khaspekov G., Kimchi A. Isolation of DAP3, a novel mediator of interferon-gamma-induced cell death. J. Biol. Chem. 1995, 270:27932-27936.
16. Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L. The small subunit of the mammalian mitochondrial ribosome: identification of the full complement of ribosomal proteins present. J. Biol. Chem. 2001, 276:19363-19374.
17. Koc E.C., Burkhart W., Blackburn K., Schlatzer D.M., Moseley A., Spremulli L.L. The large subunit of the mammalian mitochondrial ribosome: analysis of the complement of ribosomal protein present. J. Biol. Chem. 2001, 276:43958-43969.
18. Koc E.C., Ranasinghe A., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L. A new face on apoptosis: death-associated protein 3 and PDCD9 are mitochondrial ribosomal proteins. FEBS Lett. 2001, 492:166-170.
19. Kozak M. Regulation of translation via mRNA structure in prokaryotes and eukaryotes. Gene 2005, 361:13-37.
20. Kurland C. Evolution of mitochondrial genomes and the genetic code. Bioessays 1992, 14:709-714.
21. Lestienne P. Mitochondrial and nuclear DNA complementation in the respiratory chain function and defects. Biochimie 1990, 71:1115-1123.
22. Levshenkova E.V., Ukraintsev K.E., Orlova V.V., Alibaeva R.A., Kovriga I.E., Zhugdernamzhilyn O., Frolova E.I. The structure and specific features of the cDNA expression of the human gene MRPL37. Bioorg. Khim. 2004, 30:499-506.
23. Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408.
24. Lyng H., Brovig R.S., Svendsrud D.H., Holm R., Kaalhus O., Knutstad K., Oksefjell H., Sundfor K., Kristensen G.B., Stokke T. Gene expressions and copy numbers associated with metastatic phenotypes of uterine cervical cancer. BMC Genom. 2006, 7:268.
25. Mariani L., Beaudry C., McDonough W.S., Hoelzinger D.B., Kaczmarek E., Ponce F., Coons S.W., Giese A., Seiler R.W., Berens M.E. Death-associated protein 3 (Dap-3) is overexpressed in invasive glioblastoma cells in vivo and in glioma cell lines with induced motility phenotype in vitro. Clin. Cancer Res. 2001, 7:2480-2489.
26. Mariottini P., Shah Z.H., Toivonen J., Bagni C., Spelbrink J., Amaldi F., Jacobs H. Expression of the gene for mitoribosomal protein S12 is controlled in human cells at the levels of transcription, RNA splicing, and translation. J. Biol. Chem. 1999, 274:31853-31862.
27. Miller C., Saada A., Shaul N., Shabtai N., Ben-Shalom E., Shaag A., Hershkovitz E., Elpeleg O. Defective mitochondrial translation caused by a ribosomal protein (MRPS16) mutation. Ann. Neurol. 2004, 56:734-738.
28. Miller J.L., Cimen H., Koc H., Koc E.C. Phosphorylated proteins of the mammalian mitochondrial ribosome: implications in protein synthesis. J. Proteome Res. 2009, 8:4789-4798.
29. Miller J.L., Koc H., Koc E.C. Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. Protein Sci. 2008, 17:251-260.
30. Miyazaki T., Reed J.C. A GTP-binding adapter protein couples TRAIL receptors to apoptosis-inducing proteins. Nat. Immunol. 2001, 2:493-500.
31. Miyazaki T., Shen M., Fujikura D., Tosa N., Kon S., Uede T., Reed J.C. Functional role of death associated protein 3 (DAP3) in anoikis. J. Biol. Chem. 2004, 279:44667-44672.
32. Mukamel Z., Kimchi A. Death-associated protein 3 localizes to the mitochondria and is involved in the process of mitochondrial fragmentation during cell death. J. Biol. Chem. 2004, 279:36732-36738.
33. Nagata S. Apoptosis by death factor. Cell 1997, 88:355-365.
34. O'Brien T.W., O'Brien B.J., Norman R.A. Nuclear MRP genes and mitochondrial disease. Gene 2005, 354:147-151.
35. Robbins P.F., el-Gamil M., Li Y.F., Topalian S.L., Rivoltini L., Sakaguchi K., Appella E., Kawakami Y., Rosenberg S.A. Cloning of a new gene encoding an antigen recognized by melanoma-specific HLA-A24-restricted tumor-infiltrating lymphocytes. J. Immunol. 1995, 154:5944-5950.
36. Saveanu C., Fromont-Racine M., Harington A., Ricard F., Namane A., Jacquier A. Identification of 12 new yeast mitochondrial ribosomal proteins including 6 that have no prokaryotic homologues. J. Biol. Chem. 2001, 276:15861-15867.
37. Su A.I., Wiltshire T., Batalov S., Lapp H., Ching K.A., Block D., Zhang J., Soden R., Hayakawa M., Kreiman G., Cooke M.P., Walker J.R., Hogenesch J.B. A gene atlas of the mouse and human protein-encoding transcriptomes. Proc. Natl. Acad. Sci. USA 2004, 101:6062-6067.
38. Sharma M.R., Koc E.C., Datta P.P., Booth T.M., Spremulli L.L., Agrawal R.K. Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 2003, 115:97-108.
39. Takeda S., Iwai A., Nakashima M., Fujikura D., Chiba S., Li H.M., Uehara J., Kawaguchi S., Kaya M., Nagoya S., Wada T., Yuan J., Rayter S., Ashworth A., Reed J.C., Yamashita T., Uede T., Miyazaki T. LKB1 is crucial for TRAIL-mediated apoptosis induction in osteosarcoma. Anticancer Res. 2007, 27:761-768.
40. Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H., Farquhar M.G. HNOA1 interacts with complex I and DAP3 and regulates mitochondrial respiration and apoptosis. J. Biol. Chem. 2009, 284:5414-5424.
41. Toivonen J.M., Manjiry S., Touraille S., Alziari S., O'Dell K.M., Jacobs H.T. Gene dosage and selective expression modify phenotype in a Drosophila model of human mitochondrial disease. Mitochondrion 2003, 3:83-96.
42. Wallace D. Diseases of the mitochondrial DNA. Ann. Rev. Biochem. 1992, 61:1175-1212.
43. +-dependent deacetylase, SIRT3, regulates mitochondrial protein synthesis by deacetylation of mitochondrial ribosomal protein MRP-L10. J. Biol. Chem. 2009, December 30. [Epub ahead of print].
44. Yasumura K., Sugimura I., Igarashi K., Kakinuma S., Nishimura M., Doi M., Shimada Y. Altered expression of Tfg and Dap3 in Ikaros-defective T-cell lymphomas induced by X-irradiation in B6C3F1 mice. Brit. J. Haematol. 2004, 124:179-185.
45. Yoo Y.A., Kim M.J., Park J.K., Chung Y.M., Lee J.H., Chi S.G., Kim J.S., Yoo Y.D. Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1. Mol. Cell Biol. 2005, 25:6603-6616.