Preferencje help
Polish version English version Język
Widoczny [Schowaj] Abstrakt
Liczba wyników

Znaleziono wyników: 11

Liczba wyników na stronie
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników

Wyniki wyszukiwania

Wyszukiwano:
w słowach kluczowych:  ribosomal protein
help Sortuj według:

help Ogranicz wyniki do:
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
1

Genomic distribution of genes encoding 68 cytoplasmic ribosomal protein families in rice

100%
Agarwal S. M., Jain M., Grover A.
Acta Physiologiae Plantarum
|
2005
|
tom 27
|
nr 4A
Completion of rice genome sequencing has necessitated identification of transcripts encoded by the genome and their corresponding functions. In the present study we have catalogued cytoplasmic ribosomal protein complement of rice genome corresponding to 68 families. Mining TIGR (The Institute for Genomic Research) rice database and unigene sequences available from National Centre for Biotechnology Information (NCBI) produced a non-redundant set of these sequences. This resulted in identification of 209 candidate r-proteins of which 22 have not been reported previously. The number of genes per family ranges from 1 to 8 distributed throughout the genome with maximum occurrence at chromosome 7. Mapping of r-proteins on BAC clones revealed several small clusters of genes. Unigene sequences correspondtng to most of the reported r-proteins were identified indicating these genes are being expressed.
2

Ribosomal proteins L34 and S29 of amphioxus Branchiostoma belcheri tsingtauense: cDNAs cloning and gene copy number

100%
Liu L., Zhang S., Liu Z., Li H., Liu M., Wang Y., Ma L.
Acta Biochimica Polonica
|
2005
|
tom 52
|
nr 4
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.
3

Functional and physical interactions of Krr1p, a Saccharomyces cerevisiae nucleolar protein

84%
Gromadka R., Karkusiewicz I., Rempola B., Rytka J.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
The Krr1 protein of Saccharomyces cerevisiae is involved in processing of pre-rRNA and assembly of pre-ribosomal 40S subunits. To further investigate the function of Krr1p we constructed a conditional cold sensitive mutant krrl-21, and isolated seven genes from Schizosaccharomyces pombe whose products suppressed the cold sensitive phenotype of krrl-21 cells. Among the multicopy suppressors we found genes coding for translation elongation factor EF-1a, a putative ribose methyltransferase and five genes encoding ribosomal proteins. Using the tandem af­finity purification (TAP) method we identified thirteen S. cerevisiae ribosomal pro­teins interacting with Krr1p. Taken together, these results indicate that Krr1p inter­acts functionally as well as physically with ribosomal proteins. Northern blot analy­sis revealed that changes in the level of krrl-21 mRNA were accompanied by similar changes in the level of mRNAs of genes encoding ribosomal proteins. Thus, Krr1p and the genes encoding ribosomal proteins it interacts with seem to be coordinately regulated at the level of transcription.
4

Phosphorylation of yeast ribosomal proteins by CKI and CKII in the presence of heparin

84%
Wojda I., Cytrynska M., Frajnt M., Jakubowicz T.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 1
We have found that heparin has a different effect on Trichosporon cutaneum ribosomal protein phosphorylation by CKI and by CKII. In the presence of heparin, modification of 13 kDa, 19 kDa and 38 kDa proteins catalyzed by CKII was inhibited, while in the case of CKI, in addition to protein of 15 kDa, phosphorylation of 20 kDa and 35 kDa proteins was detected. It was also found that, in the presence of heparin, phosphorylation of P proteins (13 kDa and 38 kDa) by ribosome-bound protein kinases was inhibited. Moreover at the same conditions modification of 40 kDa protein was observed in all four yeast species tested.
5

Early changes in mRNA populations in leaves of ultraviolet-B-treated European beech [Fagus sylvatica L.] seedlings

84%
Ernst D., Liegl I., Kiefer E., Seidlitz H. K., Heller W., Sandermann H.
Acta Physiologiae Plantarum
|
2001
|
tom 23
|
nr 3
6

Extraribosomal function of the acidic ribosomal P1-protein YP1alpha from Saccharomyces cerevisiae

84%
Tchorzewski M., Boldyreff B., Grankowski N.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
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.
7

De novo synthesis of protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A) during oocyte maturation

67%
Chuderland D., Dvashi Z., Kaplan-Kraicer R., Ben-Meir D., Shalgi R., Lavi S.
Cellular and Molecular Biology Letters
|
2012
|
tom 17
|
nr 3
Oocyte maturation in mammals is a multiple-stage process that generates fertilizable oocytes. Ovarian oocytes are arrested at prophase of the first meiotic division characterized by the presence of a germinal vesicle. Towards ovulation, the oocytes resume meiosis and proceed to the second metaphase in a process known as maturation; they undergo nuclear and cytoplasmic changes that are accompanied by translation and degradation of mRNA. Protein phosphatase 1A, magnesium dependent, alpha isoform (PPM1A), which belongs to the metal-dependent serine/threonine protein phosphatase family, is highly conserved during evolution. PPM1A plays a significant role in many cellular functions such as cell cycle progression, apoptosis and cellular differentiation. It works through diverse signaling pathways, including p38 MAP kinase JNK and transforming growth factor beta (TGF-β). Herein we report that PPM1A is expressed in mouse oocytes and that its mRNA level rises during oocyte maturation. Using quantitative real-time polymerase chain reaction (qPCR) and western blot analysis, we found that PPM1A mRNA is synthesized at the beginning of the maturation process and remains elevated in the mature oocytes, promoting the accumulation of PPM1A protein. Since PPM1A function is mainly affected by its level, we propose that it might have an important role in oocyte maturation.
8

Increased expression of ribosomal protein S2 in liver tumors, posthepactomized livers, and proliferating hepatocytes in vitro

67%
Kowalczyk P., Woszczynski M., Ostrowski J.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 3
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.
9

SDS-PAGE characteristics of protein kinases tightly associated with chick embryo brain ribosomes

67%
Sanecka-Obacz M.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 4
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.
10

The effect of vanadate on Pichia pastoris growth, protein kinase A activity and ribosomal protein phosphorylation

67%
Frajnt M., Cytrynska M., Jakubowicz T.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
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.
11

Protein kinases CKI and CKII are implicated in modification of ribosomal proteins of the yeast Trichosporon cutaneum

67%
Wojda I., Cytrynska M., Frajnt M., Jakubowicz T.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
Phosphorylation of acidic ribosomal proteins P1/P2-P0 is a common phenomenon in eukaryotic organisms. It was found previously that in Trichosporon cutaneum, un­like in other yeast species, in addition to the two acidic ribosomal proteins, two other proteins of 15 kDa and 19 kDa of the small ribosomal subunit were phosphorylated. Here we describe two protein kinases: CKI and CKII, which are engaged in the modifi­cation of T. cutaneum ribosomal proteins. The acidic ribosomal proteins and the pro­tein of 19 kDa were modified by CKII associated with ribosomes, while the protein of 15 kDa was modified by CKI. Protein kinase CKI was purified from cell-free extract (CKIC) and from ribosomal fraction (CKIR). The molecular mass of CKIC was estab­lished at 33 kDa while that of CKIR at 35-37 kDa. A protein of 40 kDa copurified with CKIR but not CKIC. Heparin significantly in­creased 40 kDa protein phosphorylation level by CKIR. Microsequencing analysis re­vealed the presence of CKI recognition motifs in the N-terminal fragment of the 40 kDa protein.
Pierwsza strona wyników Pięć stron wyników wstecz Poprzednia strona wyników Strona / 1 Następna strona wyników Pięć stron wyników wprzód Ostatnia strona wyników
JavaScript jest wyłączony w Twojej przeglądarce internetowej. Włącz go, a następnie odśwież stronę, aby móc w pełni z niej korzystać.