Analysis of Phosphorylation of Wheat Elongation Factor 1β and β′ by Casein Kinase II

Matsumoto, Shogo; Mizoguchi, Tsuyoshi; Oizumi, Naoto; Tsuruga, Mie; Shinozaki, Kazuo; Taira, Hideharu; Ejiri, Shin-ichiro

doi:10.1271/bbb.57.1740

Cited by 10 publications

(5 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…4), as observed previously in wheat and rice eEF1Bα subunits [7,8]. This observation suggests that, similarly to the wheat eEF1Bα [16,17], the Arabidopsis eEF1Bα subunits are probably not phosphorylated by casein kinase II. Whether plant eEF1 relies on other different regulatory mechanisms remains to be determined.…”

Section: Resultssupporting

confidence: 82%

Molecular cloning and characterization of the Arabidopsis thaliana α‐subunit of elongation factor 1B

Héricourt

Jupin

1999

FEBS Letters

View full text Add to dashboard Cite

Using a PCR-based approach, we have isolated two Arabidopsis thaliana cDNA clones (K K1 and K K2) encoding the K Ksubunit of translation elongation factor 1B (eEF1BK K). They encode open reading frames of 228 and 224 amino acids respectively, with extensive homology to eEF1BK K subunits from different organisms, particularly in the C-terminal half of the protein. They both lack a conserved phosphorylation site that has been implicated in regulating nucleotide exchange activity. Using a plasmid shuffling experiment, we demonstrated that both K K1 and K K2 clones are able to complement a mutant yeast strain deficient for the eEF1BK K subunit. This provides evidence that Arabidopsis encodes at least two functional isoforms of this subunit, termed eEF1BK K1 and eEF1BK K2. A third cDNA clone was isolated that appeared to result from an alternative splicing event of the eEF1BK K1 gene.z 1999 Federation of European Biochemical Societies.

show abstract

Section: Resultssupporting

confidence: 82%

Molecular cloning and characterization of the Arabidopsis thaliana α‐subunit of elongation factor 1B

Héricourt

Jupin

1999

FEBS Letters

View full text Add to dashboard Cite

show abstract

“…One protein identified in this study is fructose-1,6bisphosphatase (FBPase, spots 18,19). BLAST searches of the amino acid sequences from the A. thaliana and Pisum sativum homologs identified indicated that this is the chloroplastic isoform of the enzyme (data not shown).…”

Section: Discussionmentioning

confidence: 83%

Analysis of desiccation‐induced candidate phosphoproteins from Craterostigma plantagineum isolated with a modified metal oxide affinity chromatography procedure

et al. 2008

View full text Add to dashboard Cite

Reversible protein phosphorylation/dephosphorylation is crucial for regulation of many cellular events, and increasing evidence indicates that this post-translational modification is also involved in the complex process of acquisition of desiccation tolerance. To analyze the phosphoproteome of the desiccation tolerant resurrection plant Craterostigma plantagineum, MOAC-enriched proteins from leaves at different stages of a de-/rehydration cycle were separated by 2-D PAGE and detected by phosphoprotein-specific staining. Using this strategy 20 putative phosphoproteins were identified by MALDI-TOF MS and MS/MS, which were not detected when total proteins were analyzed. The characterized desiccation-related phosphoproteins CDeT11-24 and CDeT6-19 were used as internal markers to validate the specificity of the analyses. For 16 of the identified proteins published evidence suggests that they are phosphoproteins. Comparative analysis of the 2-D gels showed that spot intensities of most identified putative phosphoproteins change during the de-/rehydration cycle. This suggests an involvement of these proteins in desiccation tolerance. Nearly all changes in the phosphoproteome of C. plantagineum, which are triggered by dehydration, are reversed within 4 days of rehydration, which is in agreement with physiological observations. Possible functions of selected proteins are discussed in the context of the de-/rehydration cycle.

show abstract

“…Consistent with their capacity for regulation, elongation factors exist in both phosphorylated and dephosphorylated forms. Several protein kinases have been shown to phosphorylate EF‐1 both in vivo and in vitro (Venema et al ., 1991; Matsumoto et al ., 1993; Peters et al ., 1995; Minella et al ., 1998). CKII and PKC phosphorylations appear to have opposite effects on the nucleotide exchange activity of this factor.…”

Section: Discussionmentioning

confidence: 99%

Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1β and inhibits its PKC‐mediated nucleotide exchange activity in vitro

Mamoun

Goldberg²

2001

Molecular Microbiology

View full text Add to dashboard Cite

The elongation step of protein synthesis involves binding of aminoacyl-tRNA to the ribosomal A site, formation of a peptide bond and translocation of the newly formed peptidyl-tRNA to the P site. The nucleotide exchange factor EF-1beta plays a major role in the regulation of this process by regenerating a GTP-bound EF-1alpha necessary for each elongation cycle. EF-1beta has been shown to be phosphorylated and its phosphorylation is critical for optimal activity. We have previously identified a serine/threonine protein phosphatase 2C (PP2C) from the human malaria parasite Plasmodium falciparum. In the current work, we performed Far-Western analysis to identify PfPP2C substrates. Several components of the translation and transcription machinery were identified, including translation elongation factor 1-beta (PfEF-1beta). PfEF-1beta is efficiently phosphorylated by protein kinase C and this phosphorylation results in a 400% increase in its nucleotide exchange activity. PKC-phosphorylated PfEF-1beta is readily and selectively dephosphorylated by recombinant and native PfPP2C, which downregulates the nucleotide exchange activity to its basal level. The identification of a translation elongation component as substrate for PP2C suggests an important regulatory function for this enzyme and suggests that it may be a good target for drug design in the fight against malaria.

show abstract

Analysis of Phosphorylation of Wheat Elongation Factor 1β and β′ by Casein Kinase II

Cited by 10 publications

References 5 publications

Molecular cloning and characterization of the Arabidopsis thaliana α‐subunit of elongation factor 1B

Molecular cloning and characterization of the Arabidopsis thaliana α‐subunit of elongation factor 1B

Analysis of desiccation‐induced candidate phosphoproteins from Craterostigma plantagineum isolated with a modified metal oxide affinity chromatography procedure

Plasmodium protein phosphatase 2C dephosphorylates translation elongation factor 1β and inhibits its PKC‐mediated nucleotide exchange activity in vitro

Contact Info

Product

Resources

About