Eukaryotic translation elongation factor 1 alpha 1
Elongation factor 1-alpha 1 (eEF1a1) is a protein that in humans is encoded by the EEF1A1 gene.[1][2]
This gene encodes an isoform of the alpha subunit of the elongation factor-1 complex, which is responsible for the enzymatic delivery of aminoacyl tRNAs to the ribosome. This isoform (alpha 1) is expressed in brain, placenta, lung, liver, kidney, and pancreas, and the other isoform (alpha 2) is expressed in brain, heart and skeletal muscle. This isoform is identified as an autoantigen in 66% of patients with Felty's syndrome. This gene has been found to have multiple copies on many chromosomes, some of which, if not all, represent different pseudogenes.[3]
In addition to its role in translation, eEF1a has been shown to be play a central role in the nuclear export of proteins. VHL, PABP1 and other proteins containing a TD-NEM (Transcription Dependent Nuclear Export Motif) are exported by eEF1a in a manner that is dependent on ongoing RNA polymerase II (RNA PolII)-dependent transcription.[4][5]
Interactions
Eukaryotic translation elongation factor 1 alpha 1 has been shown to interact with PLCG1.[6]
References
- ^ Lund A, Knudsen SM, Vissing H, Clark B, Tommerup N (Jan 1997). "Assignment of human elongation factor 1alpha genes: EEF1A maps to chromosome 6q14 and EEF1A2 to 20q13.3". Genomics 36 (2): 359–61. doi:10.1006/geno.1996.0475. PMID 8812466.
- ^ Wende H, Volz A, Ziegler A (Sep 2000). "Extensive gene duplications and a large inversion characterize the human leukocyte receptor cluster". Immunogenetics 51 (8-9): 703–13. doi:10.1007/s002510000187. PMID 10941842.
- ^ "Entrez Gene: EEF1A1 eukaryotic translation elongation factor 1 alpha 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1915.
- ^ Lee S, Neumann M, Stearman R, Stauber R, Pause A, Pavlakis GN, Klausner RD. (1999). "Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor protein.". Mol Cell Biol. 19 (2): 1486–97. PMC 116077. PMID 9891082. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=116077.
- ^ Khacho M, Mekhail K, Pilon-Larose K, Pause A, Côté J, Lee S. (2008). "eEF1A is a novel component of the mammalian nuclear protein export machinery.". Mol Biol Cell 19 (12): 5296–308. doi:10.1091/mbc.E08-06-0562. PMC 2592675. PMID 18799616. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2592675.
- ^ Chang, Jong-Soo; Seok Heon, Kwon Taeg-Kyu, Min Do Sik, Ahn Bong-Hyun, Lee Young Han, Suh Ju-Won, Kim Jong-Woo, Iwashita Shintaro, Omori Akira, Ichinose Sachiyo, Numata Osamu, Seo Jeong-Kon, Oh Yong-Seok, Suh Pann-Ghill (May. 2002). "Interaction of elongation factor-1alpha and pleckstrin homology domain of phospholipase C-gamma 1 with activating its activity". J. Biol. Chem. (United States) 277 (22): 19697–702. doi:10.1074/jbc.M111206200. ISSN 0021-9258. PMID 11886851.
Further reading
- Madsen HO, Poulsen K, Dahl O, et al. (1990). "Retropseudogenes constitute the major part of the human elongation factor 1 alpha gene family.". Nucleic Acids Res. 18 (6): 1513–6. doi:10.1093/nar/18.6.1513. PMC 330519. PMID 2183196. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=330519.
- Bec G, Kerjan P, Zha XD, Waller JP (1990). "Valyl-tRNA synthetase from rabbit liver. I. Purification as a heterotypic complex in association with elongation factor 1.". J. Biol. Chem. 264 (35): 21131–7. PMID 2556394.
- Uetsuki T, Naito A, Nagata S, Kaziro Y (1989). "Isolation and characterization of the human chromosomal gene for polypeptide chain elongation factor-1 alpha.". J. Biol. Chem. 264 (10): 5791–8. PMID 2564392.
- Whiteheart SW, Shenbagamurthi P, Chen L, et al. (1989). "Murine elongation factor 1 alpha (EF-1 alpha) is posttranslationally modified by novel amide-linked ethanolamine-phosphoglycerol moieties. Addition of ethanolamine-phosphoglycerol to specific glutamic acid residues on EF-1 alpha.". J. Biol. Chem. 264 (24): 14334–41. PMID 2569467.
- Motorin YuA , Wolfson AD, Orlovsky AF, Gladilin KL (1988). "Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor.". FEBS Lett. 238 (2): 262–4. doi:10.1016/0014-5793(88)80492-7. PMID 3169261.
- Ann DK, Wu MM, Huang T, et al. (1988). "Retinol-regulated gene expression in human tracheobronchial epithelial cells. Enhanced expression of elongation factor EF-1 alpha.". J. Biol. Chem. 263 (8): 3546–9. PMID 3346208.
- Brands JH, Maassen JA, van Hemert FJ, et al. (1986). "The primary structure of the alpha subunit of human elongation factor 1. Structural aspects of guanine-nucleotide-binding sites.". Eur. J. Biochem. 155 (1): 167–71. doi:10.1111/j.1432-1033.1986.tb09472.x. PMID 3512269.
- Opdenakker G, Cabeza-Arvelaiz Y, Fiten P, et al. (1987). "Human elongation factor 1 alpha: a polymorphic and conserved multigene family with multiple chromosomal localizations.". Hum. Genet. 75 (4): 339–44. doi:10.1007/BF00284104. PMID 3570288.
- Rao TR, Slobin LI (1986). "Structure of the amino-terminal end of mammalian elongation factor Tu.". Nucleic Acids Res. 14 (5): 2409. doi:10.1093/nar/14.5.2409. PMC 339668. PMID 3960725. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=339668.
- Carvalho MD, Carvalho JF, Merrick WC (1984). "Biological characterization of various forms of elongation factor 1 from rabbit reticulocytes.". Arch. Biochem. Biophys. 234 (2): 603–11. doi:10.1016/0003-9861(84)90310-2. PMID 6568109.
- Shen R, Su ZZ, Olsson CA, Fisher PB (1995). "Identification of the human prostatic carcinoma oncogene PTI-1 by rapid expression cloning and differential RNA display.". Proc. Natl. Acad. Sci. U.S.A. 92 (15): 6778–82. doi:10.1073/pnas.92.15.6778. PMC 41412. PMID 7542776. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=41412.
- Reed VS, Wastney ME, Yang DC (1995). "Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha.". J. Biol. Chem. 269 (52): 32932–6. PMID 7806521.
- Kielbassa K, Müller HJ, Meyer HE, et al. (1995). "Protein kinase C delta-specific phosphorylation of the elongation factor eEF-alpha and an eEF-1 alpha peptide at threonine 431.". J. Biol. Chem. 270 (11): 6156–62. doi:10.1074/jbc.270.11.6156. PMID 7890750.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Wu-Baer F, Lane WS, Gaynor RB (1996). "Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA.". J. Biol. Chem. 271 (8): 4201–8. doi:10.1074/jbc.271.8.4201. PMID 8626763.
- Sanders J, Brandsma M, Janssen GM, et al. (1996). "Immunofluorescence studies of human fibroblasts demonstrate the presence of the complex of elongation factor-1 beta gamma delta in the endoplasmic reticulum.". J. Cell. Sci. 109 ( Pt 5): 1113–7. PMID 8743958.
- Welle S, Thornton C, Bhatt K, Krym M (1997). "Expression of elongation factor-1 alpha and S1 in young and old human skeletal muscle.". J. Gerontol. A Biol. Sci. Med. Sci. 52 (5): B235–9. PMID 9310071.
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
- Sheu GT, Traugh JA (1998). "Recombinant subunits of mammalian elongation factor 1 expressed in Escherichia coli. Subunit interactions, elongation activity, and phosphorylation by protein kinase CKII.". J. Biol. Chem. 272 (52): 33290–7. doi:10.1074/jbc.272.52.33290. PMID 9407120.
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| Ribosomal proteins |
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Archaeal
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aIF1 · aIF2 · aIF5 · aIF6
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eIF1 (EIF1AX, AY, 1B)
eIF2 (EIF2S1, EIF2S2, EIF2S3) · EIF2B1, EIF2B2, EIF2B3, EIF2B4, EIF2B5 · EIF-2 kinase
eIF3 (EIF3A, B, C, D, F, G, H, I, J, K, M, S6)
eIF4 (EIF4A2, A3, B, E1, E2, G1, G2, G3, H)
eIF5 (EIF5A, A2, B)
eIF6 (EIF6)
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Other
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| Other concepts |
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see also disorders of translation and posttranslational modification
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)
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