| 1. |
- Abramczyk, Olga, et al.
(författare)
-
The protein kinase 60S is a free catalytic CK2alpha' subunit and forms an inactive complex with superoxide dismutase SOD1
- 2003
-
Ingår i: Biochemical and Biophysical Research Communications - BBRC. - 0006-291X .- 1090-2104. ; 307:1, s. 31-40
-
Tidskriftsartikel (refereegranskat)abstract
- The 60S ribosomes from Saccharomyces cerevisiae contain a set of acidic P-proteins playing an important role in the ribosome function. Reversible phosphorylation of those proteins is a mechanism regulating translational activity of ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. The PK60S kinase was one of the enzymes phosphorylating P-proteins. The enzyme has been purified from yeast and characterised. Pure enzyme has properties similar to those reported for casein kinase type 2. Peptide mass fingerprinting (PMF) has identified the PK60S as a catalytic alpha(') subunit of casein kinase type 2 (CK2alpha(')). Protein kinase activity is inhibited by SOD1 and by highly specific CK2 inhibitor-4,5,6,7-tetrabromo-benzotriazole (TBBt). The possible mechanism of regulation of CK2alpha(') activity in stress conditions, by superoxide dismutase in regulation of 80S-ribosome activity, is discussed.
|
|
| 2. |
- Kubinski, Konrad, et al.
(författare)
-
Yeast Elf1 factor is phosphorylated and interacts with protein kinase CK2
- 2006
-
Ingår i: Journal of Biochemistry and Molecular Biology. - 1225-8687 .- 0219-1024. ; 39:3, s. 311-318
-
Tidskriftsartikel (refereegranskat)abstract
- One of the biggest group of proteins influenced by protein kinase CK2 is formed by factors engaged in gene expression. Here we have reported recently identified yeast transcription elongation factor Elf1 as a new substrate for both monomeric and tetrameric forms of CK2. Elf1 serves as a substrate for both the recombinant CK2alpha' (K(m) 0.38 microM) and holoenzyme (K(m) 0.13 microM). By MALDI-MS we identified the two serine residues at positions 95 and 117 as the most probable in vitro phosphorylation sites. Coimmunoprecypitation experiments show that Elf1 interacts with catalytic (alpha and alpha') as well as regulatory (beta and beta') subunits of CK2. These data may help to elucidate the role of protein kinase CK2 and Elf1 in the regulation of transcription elongation.
|
|
| 3. |
- Masłyk, Maciej, et al.
(författare)
-
Yeast surviving factor Svf1 as a new interacting partner, regulator and in vitro substrate of protein kinase CK2
- 2008
-
Ingår i: Molecular and Cellular Biochemistry. - : Springer Science and Business Media LLC. - 0300-8177 .- 1573-4919. ; 312:1-2, s. 61-69
-
Tidskriftsartikel (refereegranskat)abstract
- Since Svf1 is phosphoprotein, we investigated whether it was a substrate for protein kinase CK2. According to the amino acid sequence Svf1 harbours 20 putative CK2 phosphorylation sites. Here, we have reported cloning, overexpression, purification and characterization of yeast Svf1 as a substrate for three forms of yeast CK2. Svf1 serves as a substrate for both the recombinant CK2alpha (K (m) 0.35 muM) and CK2alpha' (K (m) 0.18 muM) as well as CK2 holoenzyme (K (m) 1.1 muM). Different K (m) values argue that CK2beta(beta') subunit has an inhibitory effect on the activity of both CK2alpha and CK2alpha' towards surviving factor Svf1. Reconstitution of alpha'(2)betabeta' isoform of CK2 holoenzyme shows that beta/beta' subunits have regulatory effect depending on the kind of CK2 catalytic subunit. This effect was not observed in the case of alpha(2)betabeta' isoform, which may be due to interaction between Svf1 and regulatory CK2beta subunit (shown by co-immunoprecipitation experiments). Interactions between CK2 subunits and Svf1 protein may have influence on ATP as well as ATP-competitive inhibitors (TBBt and TBBz) binding. CK2 phosphorylates up to six serine residues in highly acidic peptide K(199)EVIPESDEEESSADEDDNEDEDEESGDSEEESGSEEESDSEEVEITYED(248) of the Svf1 protein in vitro. Presented data may help to elucidate the role of protein kinase CK2 and Svf1 in the regulation of cell survival pathways.
|
|
| 4. |
- Zielin„ski, Rafal, et al.
(författare)
-
Fip1 - an essential component of the Saccharomyces cerevisiae polyadenylation machinery is phosophorylated by protein kinase CK2
- 2006
-
Ingår i: Molecular and Cellular Biochemistry. - : Springer Science and Business Media LLC. - 0300-8177 .- 1573-4919. ; 286:1-2, s. 191-197
-
Tidskriftsartikel (refereegranskat)abstract
- Since Fip1 is phosphoprotein we investigated whether it is a substrate for protein kinase CK2. According to the amino acid sequence Fip1 harbours twenty putative CK2 phosphorylation sites. Here we have report characterization of Fip1 as a substrate for both forms of CK2. Fip1 serves as a substrate for both the recombinant CK2α ′ (K m 1.28 μM) and holoenzyme (K m 1.4 μM) but not for CK1. By MALDI-MS we identified the two serine residues at positions 73 and 77 as the possible in vitro phosphorylation sites. These data may help to elucidate the role of Fip1 in the mRNA 3'-OH polyadenylation process and the involvement of CK2 mediated phosphorylation in regulation of interactions and activity members of cleavage/polyadenylation factor (CPF) complex.
|
|
| 5. |
- Zielinski, Rafał, et al.
(författare)
-
Inhibition of yeast ribosomal stalk phosphorylation by Cu-Zn superoxide dismutase
- 2002
-
Ingår i: Biochemical and Biophysical Research Communications - BBRC. - 0006-291X .- 1090-2104. ; 296:5, s. 1310-1316
-
Tidskriftsartikel (refereegranskat)abstract
- Reversible phosphorylation of acidic ribosomal proteins of Saccharomyces cerevisiae is an important mechanism, regulating the number of active ribosomes. The key role in regulation of this process is played by specific, second messenger-independent protein kinases. A new protein-inhibitor regulating activity of PK60S kinase has been purified from yeast extracts and characterised. Peptide mass fingerprinting (PMF) and amino-acid sequence analysis by Post Source Decay (PSD) have identified the inhibitor as a Cu-Zn superoxide dismutase (SOD). Inhibition by SOD is competitive with respect to protein substrates-P proteins and 80S ribosome-with K(i) values of 3.7 microM for P2A protein and 0.6 microM for 80S ribosomes. A close correlation was found between the state of phosphorylation of P proteins in diauxic shift and logarithmic growth yeast cells and activity of SOD. The possible mechanism of regulation of PK60S activity, and participation of SOD protein in regulation of 80S-ribosome activity in stress conditions, is discussed.
|
|
| 6. |
- Zieliński, Tomasz G., et al.
(författare)
-
Reproducibility of sound-absorbing periodic porous materials using additive manufacturing technologies : Round robin study
- 2020
-
Ingår i: Additive Manufacturing. - : Elsevier B.V.. - 2214-8604 .- 2214-7810. ; 36
-
Tidskriftsartikel (refereegranskat)abstract
- The purpose of this work is to check if additive manufacturing technologies are suitable for reproducing porous samples designed for sound absorption. The work is an inter-laboratory test, in which the production of samples and their acoustic measurements are carried out independently by different laboratories, sharing only the same geometry codes describing agreed periodic cellular designs. Different additive manufacturing technologies and equipment are used to make samples. Although most of the results obtained from measurements performed on samples with the same cellular design are very close, it is shown that some discrepancies are due to shape and surface imperfections, or microporosity, induced by the manufacturing process. The proposed periodic cellular designs can be easily reproduced and are suitable for further benchmarking of additive manufacturing techniques for rapid prototyping of acoustic materials and metamaterials.
|
|
