Immuno-characterization of the Switch of Peptide Elongation Factors EEF1A-1/EF-1alpha and EEF1A-2/S1 in the Central Nervous System During Mouse Development

Overview

Journal Brain Res Dev Brain Res

Specialty Neurology

Date 2004 Mar 12

PMID 15013623

Citations 14

Authors

Jie Pan

Louis-Bruno Ruest

Suying Xu

Eugenia Wang

Affiliations

Soon will be listed here.

Abstract

During early postnatal development, a switch occurs between eEF1A-1/EF-1alpha and eEF1A-2/S1, homologous peptide elongation factors, in brain, heart, and skeletal muscle; eEF1A-2/S1 becomes the major form expressed in maturity. By immunofluorescent labeling, we detected both homologues in the developing brains of wild-type and wasted mutant mice, carrying a deletion in the eEF1A-2/S1 gene; we found that brain expression of eEF1A-2/S1 protein is restricted to mature, terminally differentiated neurons, and coincides with the disappearance of eEF1A-1/EF-1alpha 20 days after birth. Furthermore, no elongation factor 1A is present in wasted mutant mice neurons following the developmental switch, indicating that the genetic regulation silencing eEF1A-1/EF-1alpha is still functional.

Citing Articles

Local mitochondrial replication in the periphery of neurons requires the eEF1A1 protein and thetranslation of nuclear-encoded proteins.

Cardanho-Ramos C, Simoes R, Wang Y, Faria-Pereira A, Bomba-Warczak E, Craessaerts K iScience. 2024; 27(4):109136.

PMID: 38510136 PMC: 10951640. DOI: 10.1016/j.isci.2024.109136.

Face-valid phenotypes in a mouse model of the most common mutation in EEF1A2-related neurodevelopmental disorder.

Marshall G, Fasol M, Davies F, Le Seelleur M, Fernandez Alvarez A, Bennett-Ness C Dis Model Mech. 2024; 17(6).

PMID: 38179821 PMC: 10855229. DOI: 10.1242/dmm.050501.

Oncogenic activation of EEF1A2 expression: a journey from a putative to an established oncogene.

Patel S, Hassan M, Dixit M Cell Mol Biol Lett. 2024; 29(1):6.

PMID: 38172654 PMC: 10765684. DOI: 10.1186/s11658-023-00519-9.

Insulin-Like Growth Factor-1 Supplementation Promotes Brain Maturation in Preterm Pigs.

Christiansen L, Holmqvist B, Pan X, Holgersen K, Lindholm S, Henriksen N eNeuro. 2023; 10(4).

PMID: 36973010 PMC: 10112548. DOI: 10.1523/ENEURO.0430-22.2023.

Analysis of the Expression and Subcellular Distribution of and mRNAs during Neurodevelopment.

Wefers Z, Alecki C, Huang R, Jacob-Tomas S, Vera M Cells. 2022; 11(12).

PMID: 35741005 PMC: 9220863. DOI: 10.3390/cells11121877.

References

Kristensen P, Lund A, Clark B, Cavallius J, Merrick W . Purification and characterisation of a tissue specific elongation factor 1 alpha (EF-1 alpha 2) from rabbit muscle. Biochem Biophys Res Commun. 1998; 245(3):810-4. DOI: 10.1006/bbrc.1998.8510. View

Negrutskii B, Elskaya A . Eukaryotic translation elongation factor 1 alpha: structure, expression, functions, and possible role in aminoacyl-tRNA channeling. Prog Nucleic Acid Res Mol Biol. 1998; 60:47-78. DOI: 10.1016/s0079-6603(08)60889-2. View

Gangwani L, Mikrut M, Davis R . Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells. J Cell Biol. 1998; 143(6):1471-84. PMC: 2132977. DOI: 10.1083/jcb.143.6.1471. View

Duttaroy A, Bourbeau D, Wang X, Wang E . Apoptosis rate can be accelerated or decelerated by overexpression or reduction of the level of elongation factor-1 alpha. Exp Cell Res. 1998; 238(1):168-76. DOI: 10.1006/excr.1997.3819. View

Lee S, Leblanc A, Duttaroy A, Wang E . Terminal differentiation-dependent alteration in the expression of translation elongation factor-1 alpha and its sister gene, S1, in neurons. Exp Cell Res. 1995; 219(2):589-97. DOI: 10.1006/excr.1995.1268. View

Shiina N, Gotoh Y, Kubomura N, Iwamatsu A, Nishida E . Microtubule severing by elongation factor 1 alpha. Science. 1994; 266(5183):282-5. DOI: 10.1126/science.7939665. View

Lee S, Wolfraim L, Wang E . Differential expression of S1 and elongation factor-1 alpha during rat development. J Biol Chem. 1993; 268(32):24453-9. View

Lee S, Francoeur A, Liu S, Wang E . Tissue-specific expression in mammalian brain, heart, and muscle of S1, a member of the elongation factor-1 alpha gene family. J Biol Chem. 1992; 267(33):24064-8. View

Merrick W . Mechanism and regulation of eukaryotic protein synthesis. Microbiol Rev. 1992; 56(2):291-315. PMC: 372869. DOI: 10.1128/mr.56.2.291-315.1992. View

10.

Chamberlain J, Gibbs R, Ranier J, Nguyen P, Caskey C . Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification. Nucleic Acids Res. 1988; 16(23):11141-56. PMC: 339001. DOI: 10.1093/nar/16.23.11141. View

11.

Ruest L, Marcotte R, Wang E . Peptide elongation factor eEF1A-2/S1 expression in cultured differentiated myotubes and its protective effect against caspase-3-mediated apoptosis. J Biol Chem. 2001; 277(7):5418-25. PMC: 2803684. DOI: 10.1074/jbc.M110685200. View

12.

Khalyfa A, Bourbeau D, Chen E, Petroulakis E, Pan J, Xu S . Characterization of elongation factor-1A (eEF1A-1) and eEF1A-2/S1 protein expression in normal and wasted mice. J Biol Chem. 2001; 276(25):22915-22. DOI: 10.1074/jbc.M101011200. View

13.

Chen E, Proestou G, Bourbeau D, Wang E . Rapid up-regulation of peptide elongation factor EF-1alpha protein levels is an immediate early event during oxidative stress-induced apoptosis. Exp Cell Res. 2000; 259(1):140-8. DOI: 10.1006/excr.2000.4952. View

14.

Kahns S, Lund A, Kristensen P, Knudsen C, Clark B, Cavallius J . The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res. 1998; 26(8):1884-90. PMC: 147499. DOI: 10.1093/nar/26.8.1884. View

15.

Chambers D, Peters J, Abbott C . The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1alpha, encoded by the Eef1a2 gene. Proc Natl Acad Sci U S A. 1998; 95(8):4463-8. PMC: 22512. DOI: 10.1073/pnas.95.8.4463. View

16.

Das T, Mathur M, Gupta A, Janssen G, Banerjee A . RNA polymerase of vesicular stomatitis virus specifically associates with translation elongation factor-1 alphabetagamma for its activity. Proc Natl Acad Sci U S A. 1998; 95(4):1449-54. PMC: 19039. DOI: 10.1073/pnas.95.4.1449. View