The selenocysteine-specific elongation factor contains unique sequences that are required for both nuclear export and selenocysteine incorporation

PLoS ONE

Volumn 11, Issue 11, 2016, Pages

  Dubey, Aditi ^a,b   Copeland, Paul R ^a  

^a RUTGERS ROBERT WOOD JOHNSON MEDICAL SCHOOL   (United States)

^b NEW YORK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR; RECOMBINANT PROTEIN; SELENOCYSTEINE; SELENOCYSTEINE SPECIFIC ELONGATION FACTOR; SELENOPROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; CELL RECEPTOR; EFSEC PROTEIN, MOUSE; EXPORTIN 1 PROTEIN; KARYOPHERIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELLULAR DISTRIBUTION; CODON; CONFOCAL MICROSCOPY; CONTROLLED STUDY; IMMUNOFLUORESCENCE; IN VITRO STUDY; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN RNA BINDING; RAT; ANIMAL; ANTAGONISTS AND INHIBITORS; CELL LINE; CONSERVED SEQUENCE; GENE EXPRESSION; GENETIC TRANSFECTION; GENETICS; HUMAN; METABOLISM; MOUSE; NUCLEOCYTOPLASMIC TRANSPORT; SEQUENCE ALIGNMENT; TUMOR CELL LINE;

ACTIVE TRANSPORT, CELL NUCLEUS; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CELL LINE, TUMOR; CONSERVED SEQUENCE; GENE EXPRESSION; HUMANS; KARYOPHERINS; MICE; PEPTIDE ELONGATION FACTORS; PROTEIN DOMAINS; RATS; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECOMBINANT PROTEINS; SELENOPROTEINS; SEQUENCE ALIGNMENT; TRANSFECTION;

EID: 84993973231     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0165642     Document Type: Article

References (35)

1. Bellinger FP, Raman AV, Reeves M.A., Berry MJ. Regulation and function of selenoproteins in human disease. Biochem J 2009; 422:11-22. doi: 10.1042/BJ20090219 PMID: 19627257
2. Dubey A, Copeland P.R. (2015) The Molecular Regulation of Selenocysteine Incorporation into Proteins in Eukaryotes. In: Diversity of Selenium Functions in Health and Disease. CRC Press. pp. 31-48.
3. Small-Howard A., Morozova N, Stoytcheva Z., Forry EP, Mansell JB, Harney JW, et al Supramolecular complexes mediate selenocysteine incorporation in vivo. Mol Cell Biol 2006; 26: 2337-2346. doi: 10. 1128/MCB.26.6.2337-2346.2006 PMID: 16508009
4. Zavacki AM, Mansell JB, Chung M, Klimovitsky B., Harney JW, Berry MJ. Coupled tRNA(Sec)-depen-dent assembly of the selenocysteine decoding apparatus. Mol Cell 2003; 11: 773-781. PMID: 12667458
5. Donovan J, Caban K, Ranaweera R., Gonzales-Flores JN, Copeland PR. A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment. J Biol Chem 2008; 283: 35129-35139. doi: 10.1074/jbc.M806008200 PMID: 18948268
6. de Jesus L.A., Hoffmann PR, Michaud T, Forry E.P., Small-Howard A, Stillwell RJ, et al Nuclear assembly of UGA decoding complexes on selenoprotein mRNAs: a mechanism for eluding nonsense-mediated decay? Mol Cell Biol 2006; 26:1795-1805. doi: 10.1128/MCB.26.5.1795-1805.2006 PMID: 16478999
7. Papp LV, Lu J, Striebel F., Kennedy D, Holmgren A, Khanna KK The redox state of SECIS binding protein 2 controls its localization and selenocysteine incorporation function. Mol Cell Biol 2006; 26: 4895-4910. doi: 10.1128/MCB.02284-05 PMID: 16782878
8. Touat-Hamici Z., Legrain Y, Bulteau A.L., Chavatte L. Selective Up-Regulation of Human Selenoproteins in Response to Oxidative Stress. J Biol Chem 2014; 289:14750-14761. doi: 10.1074/jbc.M114.551994 PMID: 24706762
9. Sunde RA, Raines AM Selenium regulation of the selenoprotein and nonselenoprotein transcriptomes in rodents. Adv Nutr 2011; 2:138-150. doi: 10.3945/an.110.000240 PMID: 22332043
10. Gonzalez-Flores J.N., Gupta N, Demong L.W., Copeland PR. The selenocysteine-specific elongation factor contains a novel and multi-functional domain. J Biol Chem 2012; 287: 38936-38945. doi: 10. 1074/jbc.M112.415463 PMID: 22992746
11. Gupta N, Demong LW, Banda S, Copeland PR Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements. J Mol Biol 2013; 425: 2415-2422. doi: 10.1016/j.jmb.2013.04.016 PMID: 23624110
12. Schindelin J, Arganda-Carreras I, Frise E., Kaynig V, Longair M, Pietzsch T., et al. Fiji: an open-source platform for biological-image analysis. Nat Methods 2012; 9: 676-682. doi: 10.1038/nmeth.2019 PMID: 22743772
13. Nishi K, Yoshida M, Fujiwara D., Nishikawa M, Horinouchi S, Beppu T. Leptomycin B targets a regulatory cascade of crm1, a fission yeast nuclear protein, involved in control of higher order chromosome structure and gene expression. J Biol Chem 1994; 269: 6320-6324. PMID: 8119981
14. Yang J, Bardes ES, Moore J.D., Brennan J., Powers MA, Kornbluth S. Control of cyclin B1 localization through regulated binding of the nuclear export factor CRM1. Genes Dev 1998; 12: 2131-2143. PMID: 9679058
15. Copeland PR, Driscoll DM Purification, redox sensitivity, and RNA binding properties of SECIS-binding protein 2, a protein involved in selenoprotein biosynthesis. J Biol Chem 1999; 274: 25447-25454. PMID: 10464275
16. Fletcher JE, Copeland PR, Driscoll DM Polysome distribution of phospholipid hydroperoxide glutathione peroxidase mRNA: evidence for a block in elongation at the UGA/selenocysteine codon. RNA 2000; 6: 1573-1584. PMID: 11105757
17. Leibundgut M, Frick C, Thanbichler M., Bock A, Ban N. Selenocysteine tRNA-specific elongation factor SelB is a structural chimaera of elongation and initiation factors. EMBO J 2005; 24:11-22. doi: 10. 1038/sj.emboj.7600505 PMID: 15616587
18. Kosugi S, Hasebe M, Tomita M., Yanagawa H. Systematic identification of cell cycle-dependent yeast nucleocytoplasmic shuttling proteins by prediction of composite motifs. Proc Natl Acad Sci USA 2009; 106: 10171-10176. doi: 10.1073/pnas.0900604106 PMID: 19520826
19. Xu L, Massagué J. Nucleocytoplasmic shuttling of signal transducers. Nat Rev Mol Cell Biol 2004; 5: 209-219. doi: 10.1038/nrm1331 PMID: 14991001
20. Shalem O, Sanjana NE, Hartenian E, Shi X., Scott DA, Mikkelsen TS, et al. Genome-scale CRISPR-Cas9 knockout screening in human cells. Science 2014; 343: 84-87. doi: 10.1126/science.1247005 PMID: 24336571
21. Shetty SP, Shah R, Copeland PR Regulation of selenocysteine incorporation into the selenium transport protein, Selenoprotein P. J Biol Chem 2014; 289: 25317-25326. doi: 10.1074/jbc.M114.590430 PMID: 25063811
22. Fletcher JE, Copeland PR, Driscoll D.M., Krol A. The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2. RNA 2001; 7:1442-1453. PMID: 11680849
23. Hutten S, Kehlenbach RH CRM1-mediated nuclear export: to the pore and beyond. Trends Cell Biol 2007; 17:193-201. doi: 10.1016/j.tcb.2007.02.003 PMID: 17317185
24. Seeher S, Schweizer U. Targeted deletion of Secisbp2 reduces, but does not abrogate, selenoprotein expression and leads to striatal interneuron loss. Free Radic Biol Med 2014; 75 Suppl 1: S9.
25. Bohnsack MT, Regener K, Schwappach B., Saffrich R, Paraskeva E, Hartmann E., et al. Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm. EMBO J 2002; 21: 6205-6215. doi: 10.1093/emboj/cdf613 PMID: 12426392
26. Sunde RA, Raines AM Selenium regulation of the selenoprotein and nonselenoprotein transcriptomes in rodents. Adv Nutr 2011; 2:138-150. doi: 10.3945/an.110.000240 PMID: 22332043
27. Seeher S, Atassi T, Mahdi Y., Carlson BA, Braun D, Wirth EK, et al Secisbp2 is essential for embryonic development and enhances selenoprotein expression. Antioxid Redox Signal 2014; 21: 835-849. doi: 10.1089/ars.2013.5358 PMID: 24274065
28. Nigg EA. Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature 1997; 386:779-787. doi: 10.1038/386779a0 PMID: 9126736
29. Chung J, Khadka P, Chung IK Nuclear import of hTERT requires a bipartite nuclear localization signal and Akt-mediated phosphorylation. J Cell Sci 2012; 125: 2684-2697. doi: 10.1242/jcs.099267 PMID: 22366458
30. Marfori M, Mynott A, Ellis J.J., Mehdi AM, Saunders NF, Curmi PM, et al Molecular basis for specificity of nuclear import and prediction of nuclear localization. Biochim Biophys Acta 2011; 1813:1562-1577. doi: 10.1016/j.bbamcr.2010.10.013 PMID: 20977914
31. Fornerod M, Ohno M, Yoshida M., Mattaj IW. CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 1997; 90:1051-1060. PMID: 9323133
32. Wolff B, Sanglier JJ, Wang Y. Leptomycin B is an inhibitor of nuclear export: inhibition of nucleo-cyto-plasmic translocation of the human immunodeficiency virus type 1 (HIV-1) Rev protein and Rev-dependent mRNA. Chem Biol 1997; 4: 139-147. PMID: 9190288
33. Kudo N, Matsumori N, Taoka H., Fujiwara D, Schreiner EP, Wolff B, et al Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc Natl Acad Sci U S A 1999; 96: 9112-9117. PMID: 10430904
34. Watanabe M, Fukuda M, Yoshida M., Yanagida M, Nishida E. Involvement of CRM1, a nuclear export receptor, in mRNA export in mammalian cells and fission yeast. Genes Cells 1999; 4: 291-297. PMID: 10421839
35. Cherfils J, Zeghouf M. Chronicles of the GTPase switch. Nat Chem Biol 2011; 7: 493-495. doi: 10. 1038/nchembio.608 PMID: 21769091