Informacja

Drogi użytkowniku, aplikacja do prawidłowego działania wymaga obsługi JavaScript. Proszę włącz obsługę JavaScript w Twojej przeglądarce.

Wyszukujesz frazę "ribosomal protein" wg kryterium: Temat


Wyświetlanie 1-7 z 7
Tytuł:
The effect of vanadate on Pichia pastoris growth, protein kinase A activity and ribosomal protein phosphorylation.
Autorzy:
Frajnt, Magdalena
Cytryńska, Małgorzata
Jakubowicz, Teresa
Powiązania:
https://bibliotekanauki.pl/articles/1043701.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphorylation
vanadate
Pichia pastoris
PKA
ribosomal proteins
protein kinases
Opis:
It was found that wild type yeast Pichia pastoris can tolerate vanadate concentration as high as 25 mM in the growth medium. Moreover, four vanadate-resistant P. pastoris strains designated JC100/1, JC100/3, JC100/9 and JC100/15 exhibiting tolerance up to 150 mM vanadate were selected. Growth of P. pastoris was correlated with vanadate to vanadyl reduction and its accumulation in the growth medium. In two selected strains, JC100/9 and JC100/15, protein kinase A activity was much higher in comparison to the wild type strain even without vanadate addition to the growth medium. Moreover, in the presence of vanadate, protein kinase A activity was significantly increased in the wild type and the vanadate-resistant JC100/1 and JC100/3 strains. It was also found that phosphorylation of a 40 kDa protein associated with ribosomes occured in all vanadate-resistant strains from the logarithmic, while in the wild type strain from the stationary growth phase. From the presented results it can be concluded that a protein kinase A signalling pathway(s) might be involved in the mechanism of P. pastoris vanadate resistance. The results also indicate a possible role of the 40 kDa protein in protection of P. pastoris against vanadate toxicity.
Źródło:
Acta Biochimica Polonica; 2002, 49, 4; 959-968
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Increased expression of ribosomal protein S2 in liver tumors, posthepactomized livers, and proliferating hepatocytes in vitro.
Autorzy:
Kowalczyk, Piotr
Woszczyński, Marek
Ostrowski, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1043722.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
ribosomal protein S2
partial hepatectomy
hepatocytes
hepatocellular carcinoma
Opis:
The ribosomal protein S2 (RPS2) is encoded by a gene from the highly conserved mammalian repetitive gene family LLRep3. It participates in aminoacyl-transfer RNA binding to ribosome, potentially affecting the fidelity of mRNA translation. These studies were designed to measure the expression of RPS2 during increased cell proliferation. Using Western and Northern blot analyses, we found that the levels of RPS2 protein and its corresponding mRNA were higher in mouse hepatocellular carcinoma, in mouse livers after one-third partial hepatectomy, and in serum-starved cultured hepatocytes following serum treatment. Our study shows that the increased expression of RPS2 correlates with increased cell proliferation. However, whether the altered expression of this protein reflects its involvement in cellular proliferation or represents an associated phenomena is still a key question that needs to be explored.
Źródło:
Acta Biochimica Polonica; 2002, 49, 3; 615-624
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Cloning and characterization of the gene encoding ribosomal P0 phosphoprotein from Neurospora crassa.
Autorzy:
Krokowski, Dawid
Tchórzewski, Marek
Grankowski, Nikodem
Powiązania:
https://bibliotekanauki.pl/articles/1043800.pdf
Data publikacji:
2002
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
phosphorylation
cloning
ribosomal P0 protein
Neurospora crassa
Opis:
A gene for ribosomal protein P0 that belongs to the family of ribosomal P proteins was isolated from a Neurospora crassa cDNA library, using polyclonal antibodies against recombinant P0 protein from Saccharomyces cerevisiae. This is the first gene for ribosomal P0 protein to be cloned from filamentous fungi. The derived P0 protein sequence has a strong homology to other eukaryotic P0 proteins; yet, there is a notable alteration in the conservative C-terminal region, placing this protein among the unique sequences from protozoan parasites.
Źródło:
Acta Biochimica Polonica; 2002, 49, 1; 11-18
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Ribosomal proteins L34 and S29 of amphioxus Branchiostoma belcheri tsingtauense: cDNAs cloning and gene copy number
Autorzy:
Liu, Lina
Zhang, Shicui
Liu, Zhenhui
Li, Hongyan
Liu, Mei
Wang, Yongjun
Ma, Lifang
Powiązania:
https://bibliotekanauki.pl/articles/1041331.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
amphioxus
ribosomal protein
S29
copy number
Branchiostoma
L34
Opis:
The complete cDNA and deduced amino-acid sequences of ribosomal proteins L34 (AmphiL34) and S29 (AmphiS29) from the amphioxus Branchiostoma belcheri tsingtauense were identified in this study. The AmphiL34 cDNA is 435 nucleotides in length and encodes a 118 amino-acid protein with calculated molecular mass of 13.6 kDa. It shares 53.6-67.5% amino-acid sequence identity with its eukaryotic counterparts including human, mouse, rat, pig, frog, catfish, fruit fly, mosquito, armyworm, nematode and yeast. The AmphiS29 cDNA comprises 453 nucleotides and codes for a 56 amino-acid protein with a calculated molecular mass of 6.6 kDa. It shows 66.1-78.6% amino-acid sequence identity to eukaryotic S29 proteins from human, mouse, rat, pig, zebrafish, seahorse, fruit fly, nematode, sea hare and yeast. AmphiL34 contains a putative nucleolar localization signal, while AmphiS29 has a zinc finger-like domain. A phylogenetic tree deduced from the conserved sequences of AmphiL34 and AmphiS29 and other known counterparts indicates that the positions of AmphiL34/AmphiS29 are intermediate between the vertebrate and invertebrate L34/S29. Southern blot analysis demonstrates the presence of one copy of the L34 gene and 2-3 copies of the S29 gene in the genome of the amphioxus B. belcheri tsingtauense. This is in sharp contrast to the existence of 7-9 copies of the L34 gene and 14-17 copies of the S29 gene in the rat genome. These date suggest that housekeeping genes like AmphiL34 and AmphiS29 have undergone large-scale duplication in the chordate lineage.
Źródło:
Acta Biochimica Polonica; 2005, 52, 4; 857-862
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
SDS/PAGE characteristics of protein kinases tightly associated with chick embryo brain ribosomes
Autorzy:
Sanecka-Obacz, Maria
Powiązania:
https://bibliotekanauki.pl/articles/1044449.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein phosphorylation
chick brain development
ribosomal kinases
CK2
PKA
CK1
fetal brain
brain ribosomes
Opis:
Protein kinases tightly associated with chick embryo brain ribosomes washed with Triton X-100 and KCl were characterized by their ability to phosphorylate ribosomes and two exogenous substrates, histone IIA and casein. c-AMP-dependent kinase (PKA) and casein kinases (CK1, CK2) were examined in the presence of specific modulators by SDS/ PAGE followed by  renaturation in gel assay according to Kameshita & Fujisawa (Anal. Biochem. 1989, 183, 139-143). Basing on these data it can be presumed that PKA activity increases, but the levels of CK2 and CK1 decrease during chick embryo development.
Źródło:
Acta Biochimica Polonica; 1999, 46, 4; 911-917
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Molecular docking and pharmacokinetic prediction of phytochemicals from Syzygium cumini in interaction with penicillin-binding protein 2a and erythromycin ribosomal methylase of Staphylococcus aureus
Autorzy:
Shidiki, A.
Vyas, A.
Powiązania:
https://bibliotekanauki.pl/articles/2096259.pdf
Data publikacji:
2022
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
methicillin-resistant S. aureus
penicillin-binding protein 2a
erythromycin ribosomal methylase
Opis:
Background. MRSA and MLSB resistant S. aureus are known as important pathogens, which are responsible for many cases of both hospital and community-acquired infections worldwide. Studying drug discovery from plant sources is regarded as an important prevention strategy regarding these types of infections. Material and methods. Agar well diffusion method was performed for antimicrobial evaluation, LCMS technique used for identification of different compounds, molecular docking performed by application of iGEMDOCK for PBP2a and ERM to plant compounds, and its pharmacokinetic evaluation of ADMET through use of AdmetSAR. Results. Water extract was the most effective against resistant strains of Staphylococcus aureus. Twenty compounds belonging to phenols, flavonoids, organic acids, terpenoids groups were reported. Eighteen plant compounds passed in Lipinski's rule of five. iGEMDOCK revealed diferulic acid has the least binding energy -102.37 kcal/mole to penicillin-binding protein 2a and taxifolin has the least binding energy of -103.12 kcal/mole to erythromycin ribosomal methylase in comparison to control linezolid. These compounds raise the potential for developing potent inhibitors of penicillin-binding protein 2a and erythromycin ribosomal methylase for drug development. ADMET properties revealed that eighteen studied compounds were found in category III and IV with non-toxic properties except two butin and taxifolin found in category II with toxic properties. Conclusions. It can be concluded that diferulic acid and taxifolin compounds provide the best inhibitor effect to PBP2a and ERM protein for inhibition of MRSA and MLSB resistant strains of S. aureus through the application of molecular docking, leading to a lead drug candidate for the treatment of diseases.
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2022, 103, 1; 5-18
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Extraribosomal function of the acidic ribosomal P1-protein YP1α from Saccharomyces cerevisiae
Autorzy:
Tchórzewski, Marek
Boldyreff, Brigitte
Grankowski, Nikodem
Powiązania:
https://bibliotekanauki.pl/articles/1044447.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
acidic ribosomal P-protein
transactivation
translation
yeast
Opis:
The yeast acidic ribosomal P-proteins YP1α, YP1β, YP2a and YP2b were studied for a possible transactivation potential beside their ribosomal function. The fusions of P-proteins with the GAL4 DNA-binding domain were assayed toward their transcriptional activity with the aid of reporter genes in yeast. Two of the P-proteins, YP1α and YP1β, exhibited transactivation potential, however, only YP1α can be regarded as a potent transactivator. This protein was able to transactivate a reporter gene associated with two distinct promoter systems, GAL1 or CYC1. Additionally, truncated proteins of YP1α and YP1β were analyzed. The N-terminal part of YP1α fused to GAL4-BD showed transactivation potential but the C-terminal part did not. Our results suggest a putative extraribosomal function for these ribosomal proteins which consequently may be classified as "moonlighting" proteins.
Źródło:
Acta Biochimica Polonica; 1999, 46, 4; 901-910
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-7 z 7

    Ta witryna wykorzystuje pliki cookies do przechowywania informacji na Twoim komputerze. Pliki cookies stosujemy w celu świadczenia usług na najwyższym poziomie, w tym w sposób dostosowany do indywidualnych potrzeb. Korzystanie z witryny bez zmiany ustawień dotyczących cookies oznacza, że będą one zamieszczane w Twoim komputerze. W każdym momencie możesz dokonać zmiany ustawień dotyczących cookies