Functional characterization of PeIF5B as eIF5B homologue from Pisum sativum

We earlier reported ‘PeIF5B’ as a novel factor from Pisum sativum that has sequence similarity to eIF5B (S. Rasheedi, S. Ghosh, M. Suragani et al., P. sativum contains a factor with strong homology to eIF5B, Gene 399 (2007) 144–151). The main aim of the present study was to perform functional charac...

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Veröffentlicht in:Biochimie 2015-11, Vol.118, p.36-43
Hauptverfasser: Rasheedi, Sheeba, Suragani, Madhuri, Raviprasad, Podili, Ghosh, Sudip, Suragani, Rajasekhar N.V.S., Ramaiah, Kolluru V.A., Ehtesham, Nasreen Z.
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Sprache:eng
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Zusammenfassung:We earlier reported ‘PeIF5B’ as a novel factor from Pisum sativum that has sequence similarity to eIF5B (S. Rasheedi, S. Ghosh, M. Suragani et al., P. sativum contains a factor with strong homology to eIF5B, Gene 399 (2007) 144–151). The main aim of the present study was to perform functional characterization of PeIF5B as an eIF5B homologue from plant system. PeIF5B shows binding to Met-tRNAfMet, hydrolyses GTP and interacts with ribosomes. In vivo growth complementation analysis shows that PeIF5B partially complements its yeast homologue. Interestingly, PeIF5B mainly localizes in the nucleus as confirmed by nuclear localization signal (NLS) prediction, confocal imaging and immunoblots of cellular fractions. Similar to the yeast eIF5B but unlike the human orthologue, PeIF5B is an intron-less gene. This study highlights PeIF5B's role as a functional eIF5B homologue possibly participating in nuclear translation in plant system. •The novel protein factor from Pisum sativum (PeIF5B) shows sequence and functional similarity to other eIF5Bs.•This is the first report of the characterization of a plant eIF5B homologue.•PeIF5B shows GTP dependent tRNA binding.•PeIF5B has a nuclear localization signal.•PeIF5B gets translocated to nuclei.
ISSN:0300-9084
1638-6183
DOI:10.1016/j.biochi.2015.07.017