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Utilize este identificador para citar ou criar um link para este item: http://acervodigital.unesp.br/handle/11449/74448
Título: 
EIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer
Autor(es): 
Instituição: 
  • Universidade Estadual Paulista (UNESP)
  • Universidade Federal do ABC (UFABC)
ISSN: 
  • 0939-4451
  • 1438-2199
Resumo: 
The protein eukaryotic initiation factor 5A (eIF5A) is highly conserved among archaea and eukaryotes, but not in bacteria. Bacteria have the elongation factor P (EF-P), which is structurally and functionally related to eIF5A. eIF5A is essential for cell viability and the only protein known to contain the amino acid residue hypusine, formed by post-translational modification of a specific lysine residue. Although eIF5A was initially identified as a translation initiation factor, recent studies strongly support a function for eIF5A in the elongation step of translation. However, the mode of action of eIF5A is still unknown. Here, we analyzed the oligomeric state of yeast eIF5A. First, by using size-exclusion chromatography, we showed that this protein exists as a dimer in vitro, independent of the hypusine residue or electrostatic interactions. Protein-protein interaction assays demonstrated that eIF5A can form oligomers in vitro and in vivo, in an RNA-dependent manner, but independent of the hypusine residue or the ribosome. Finally, small-angle X-ray scattering (SAXS) experiments confirmed that eIF5A behaves as a stable dimer in solution. Moreover, the molecular envelope determined from the SAXS data shows that the eIF5A dimer is L-shaped and superimposable on the tRNAPhe tertiary structure, analogously to the EF-P monomer. © 2012 Springer-Verlag.
Data de publicação: 
1-Fev-2013
Citação: 
Amino Acids, v. 44, n. 2, p. 631-644, 2013.
Duração: 
631-644
Palavras-chaves: 
  • Dimer
  • EF-P
  • eIF5A
  • Hypusine
  • tRNA
  • dimer
  • elongation factor
  • elongation factor P
  • hypusine
  • initiation factor 5A
  • monomer
  • oligomer
  • transfer RNA
  • unclassified drug
  • cell nucleus membrane
  • dimerization
  • gel permeation chromatography
  • in vitro study
  • in vivo study
  • nonhuman
  • particle size
  • priority journal
  • protein protein interaction
  • protein tertiary structure
  • radiation scattering
  • ribosome
  • RNA structure
  • static electricity
  • yeast
  • Dimerization
  • Humans
  • Models, Molecular
  • Peptide Elongation Factors
  • Peptide Initiation Factors
  • RNA-Binding Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Eukaryota
Fonte: 
http://dx.doi.org/10.1007/s00726-012-1387-7
Endereço permanente: 
Direitos de acesso: 
Acesso restrito
Tipo: 
outro
Fonte completa:
http://repositorio.unesp.br/handle/11449/74448
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