The protein kinase 60S is a free catalytic CK2α′ subunit and forms an inactive complex with superoxide dismutase SOD1

Abramczyk, Olga; Zień, Piotr; Zieliński, Rafał; Pilecki, Marek; Hellman, Ulf; Szyszka, Ryszard

doi:10.1016/s0006-291x(03)01126-4

Cited by 23 publications

(25 citation statements)

References 68 publications

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“…Mammalian RPS19 was found to interact with mammalian orthologs (60 S ribosomal protein L3, 60 S ribosomal protein S7, and CK2␣) of three of the plant proteins identified in this work by mass spectrometry of the purified wheat germ CK2 preparation. The observations in this work support the mammalian data that suggest CK2␣ may bind to ribosomes to phosphorylate various ribosomal proteins, initiation factors, or other associated proteins of the translational machinery (32). There is some speculation that CK2 phosphorylation could also regulate ribosome assembly or the degradation of specific ribosomal proteins (33-35).…”

Section: Purification Of Native Ck2supporting

confidence: 84%

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Differential Phosphorylation of Plant Translation Initiation Factors by Arabidopsis thaliana CK2 Holoenzymes

Dennis

Browning

2009

Journal of Biological Chemistry

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A previously described wheat germ protein kinase (Yan, T. F., and Tao, M. (1982) J. Biol. Chem. 257, 7037-7043) was identified unambiguously as CK2 using mass spectrometry. CK2 is a ubiquitous eukaryotic protein kinase that phosphorylates a wide range of substrates. In previous studies, this wheat germ kinase was shown to phosphorylate eIF2␣, eIF3c, and three large subunit (60 S) ribosomal proteins (Browning, K. S., Yan, T. F., Lauer, S. J., Aquino, L. A., Tao, M., and Ravel, J. M. (1985) Plant Physiol. 77, 370 -373). To further characterize the role of CK2 in the regulation of translation initiation, Arabidopsis thaliana catalytic (␣1 and ␣2) and regulatory (␤1, ␤2, ␤3, and ␤4) subunits of CK2 were cloned and expressed in Escherichia coli. Recombinant A. thaliana CK2␤ subunits spontaneously dimerize and assemble into holoenzymes in the presence of either CK2␣1 or CK2␣2 and exhibit autophosphorylation. The purified CK2 subunits were used to characterize the properties of the individual subunits and their ability to phosphorylate various plant protein substrates. CK2 was shown to phosphorylate eIF2␣, eIF2␤, eIF3c, eIF4B, eIF5, and histone deacetylase 2B but did not phosphorylate eIF1, eIF1A, eIF4A, eIF4E, eIF4G, eIFiso4E, or eIFiso4G. Differential phosphorylation was exhibited by CK2 in the presence of various regulatory ␤-subunits. Analysis of A. thaliana mutants either lacking or overexpressing CK2 subunits showed that the amount of eIF2␤ protein present in extracts was affected, which suggests that CK2 phosphorylation may play a role in eIF2␤ stability. These results provide evidence for a potential mechanism through which the expression and/or subcellular distribution of CK2 ␤-subunits could participate in the regulation of the initiation of translation and other physiological processes in plants.

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Section: Purification Of Native Ck2supporting

confidence: 84%

“…Generally, 20 l-incubation mixtures contained 50 mM HEPES-KOH, pH 7.6, 5 mM MgCl 2 , 2.4 mM DTT, 0.2 mM [␥- 32 P]ATP (ϳ100 -250 cpm/pmol), 100 -150 mM KCl, and ϳ1 pmol of CK2. Incubation was at 30°C for 20 min or as indicated.…”

Section: Phosphorylation Of Ck2 Substratesmentioning

confidence: 99%

Differential Phosphorylation of Plant Translation Initiation Factors by Arabidopsis thaliana CK2 Holoenzymes

Dennis

Browning

2009

Journal of Biological Chemistry

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“…In S. cerevisiae, it was shown that CK2a has properties that are characteristic for the CK2 holoenzyme with some exceptions. CK2a is not inhibited by heparin and stimulated by polyamines, and it shows differences in the substrate specificity [45]. Furthermore, CK2a phosphorylates the b-subunit more rapidly and to a higher extent than CK2a [46].…”

Section: Discussionmentioning

confidence: 97%

KIF5C: A new binding partner for protein kinase CK2 with a preference for the CK2α’ subunit

Schäfer

Götz

Dudek

et al. 2008

Cell. Mol. Life Sci.

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Protein kinase CK2 is a highly conserved serine/threonine kinase that is ubiquitously expressed in eukaryotic cells. CK2 is a constitutively active tetrameric enzyme composed of two catalytic alpha and/or alpha'-subunits and two regulatory beta-subunits. There is increasing evidence that the individual subunits may have independent functions and that they are asymmetrically distributed inside the cell. To gain a better understanding of the functions of the individual subunits, we employed a yeast-two-hybrid screen with CK2alpha and CK2alpha'. We identified the motor neuron protein KIF5C as a new binding partner for CK2. The interaction found in the yeast-two-hybrid screen was confirmed by co-sedimentation analysis on a sucrose density gradient and by co-immunoprecipitation analysis. Pull-down experiments and surface plasmon resonance spectrometry revealed a direct binding of KIF5C to CK2alpha'. Co-localization studies with neuroblastoma cells, bone marrow and with primary neurons confirmed the biochemical analysis that KIF5C preferentially bound to CK2alpha'.

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“…The 60S acidic ribosomal protein P0 is a protein conserved in all eukaryotes which is the orthologue of the Escherichia coli protein L10 (Rich & Steitz 1987). Differential expression and regulation of 60S ribosomal protein P0 have been shown to be related to the cellular response to various stresses, including oxidative stress (Abramczyk et al 2003;Maniratanachote et al 2006).…”

Section: Discussionmentioning

confidence: 99%

Proteomic response of Trichoderma aggressivum f. europaeum to Agaricus bisporus tissue and mushroom compost

2014

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a b s t r a c tA cellular proteomic analysis was performed on Trichoderma aggressivum f. europaeum.Thirty-four individual protein spots were excised from 2-D electropherograms and analysed by ESI-Trap Liquid Chromatography Mass Spectrometry (LC/MS). Searches of the NCBInr and SwissProt protein databases identified functions for 31 of these proteins based on sequence homology. A differential expression study was performed on the intracellular fraction of T. aggressivum f. europaeum grown in media containing Agaricus bisporus tissue and Phase 3 mushroom compost compared to a control medium. Differential expression was observed for seven proteins, three of which were upregulated in both treatments, two were down regulated in both treatments and two showed qualitatively different regulation under the two treatments. No proteins directly relating to fungal cell wall degradation or other mycoparasitic activity were observed. Functions of differentially produced intracellular proteins included oxidative stress tolerance, cytoskeletal structure, and cell longevity. Differential production of these proteins may contribute to the growth of T. aggressivum in mushroom compost and its virulence toward A. bisporus.

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The protein kinase 60S is a free catalytic CK2α′ subunit and forms an inactive complex with superoxide dismutase SOD1

Cited by 23 publications

References 68 publications

Differential Phosphorylation of Plant Translation Initiation Factors by Arabidopsis thaliana CK2 Holoenzymes

Differential Phosphorylation of Plant Translation Initiation Factors by Arabidopsis thaliana CK2 Holoenzymes

KIF5C: A new binding partner for protein kinase CK2 with a preference for the CK2α’ subunit

Proteomic response of Trichoderma aggressivum f. europaeum to Agaricus bisporus tissue and mushroom compost

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