Wyniki wyszukiwania

1

Probing the anticodon loop structure in yeast tRNAphey with single strand-specific nuclease S1

100%

Marciniec T., Ciesiolka J., Krzyzosiak W.

Acta Biochimica Polonica

|

1989

|

tom 36

|

nr 2

2

The activity of aminoacyl-tRNA synthetases in stomach cancer

100%

Pasternak K., Paluszkiewicz P., Borkowski T.

Applied Biology Communications. Lublin Scientific Center

|

1993

|

tom 03

|

nr 5-6

3

Two intron-containing pre-tRNAsTyr from Triticum aestivum are efficiently processed and spliced in homologous cell-free extract

100%

Szweykowska-Kulinska Z.

Acta Biochimica Polonica

|

1992

|

tom 39

|

nr 3

Two wheat pre-tRNAsTyr containing introns and flanks are accurately and efficiently spliced in homologous wheat germ S23 extract. The initiation and termination sites upon in vitro transcription in HeLu cell extract have been estimated for both pre-tRNAs.

4

Is the tRNA ochre suppressor supX derived from gltT ?

100%

Plachta A., Janion C.

Acta Biochimica Polonica

|

1992

|

tom 39

|

nr 3

Some of the argE3 —>Arg+ revertants .show supX suppressor activity. The genetic relationship of.1KupX is not yet known hut the evidences are presented, that supX does not derive from gltT encoding tRN Glu/UUG-

5

Rapid separation of tyrosine - specific tRNA from white lupin

100%

Barciszewska M. Z., Krajewski J., Gawronska I., Barciszewski J.

Acta Biochimica Polonica

|

1992

|

tom 39

|

nr 2

During Isolation of total rilmnucleic acids from white lupin (Lupinus albus) and their subsequent separation by 10% polyacrylamide gel electrophoresis, a fast migrating RNA band is very well separated. The nucleotide sequence analysis of 76 nucleotide long sequence with many modified nucleosides was found to be identical with that of tyrosine specific tRNA of yellow lupin seeds (Lupinus luteus) and wheat germ (Trtiicum aestivum). Also this tRNATyr is identical with plant amber suppressor tRNA. 'I'he presented approach offers a very rapid method of purification of plant tRNA with UAG suppressor activity.

6

Nowo poznane funkcje transferowych kwasow rybonukleinowych i mozliwosci ich wykorzystania w biotechnologii

88%

Barciszewska M. Z., Barciszewski J.

Biotechnologia

|

1992

|

nr 1

63-75

7

The response of the double strand-specific nuclease V1 to Y-base removal in yeast tRNA(Phe)

88%

Marciniec T., Ciesiolka J., Krzyzosiak W.

Acta Biochimica Polonica

|

1989

|

tom 36

|

nr 2

8

Pozakomórkowa obecność aminoacylo-tRNA syntetaz

88%

Pasternak K.

Biuletyn Magnezologiczny

|

1997

|

tom 02

|

nr 2

139-141

Aminoacyl-tRNA synthetases (ARS) in consideration of the key role that they play in the process of protein biosynthesis, have caused specialinterest. They have been isolated and their properties have been tested in samples from plants, bacteria and animals. Aside from their differences in structure and form, they fulfil their function as specific aminoacylation tRNA. ARS in the cell are found mainly in the cytosol, but are also found in mitochondria. Until now extra-cellular ARS have not been observed. In the last few years however, there have been reports of ARS antibodies in the blood serum of patients with certain autoagressive diseases. These reasons resulted in the conduct of tests with the following goals: 1. the attempt to find extra-cellular ARS 2. analysing the possibility of liberating ARS from the cell 3. explaining the lack of ARS enzymatic activity in blood serum. Initially ARS activity in human physiological and pathological (gross organ damage) blood serums was tested. No enzymatic activity was observed in either complete blood serum or in their fractions. The lack of enzyme activity did not necessarily indicate that ARS was not present in blood serum. Tests were conducted in order to determine the presence of ARS by immunological methods. ARS samples were obtained from human tissues taken of a surgical clinic and then used to immunize rabbits. The serum thereby obtained contained antibodies that reacted with the fraction of free ARS and the macromollecular complex fraction. By using the technics of immunodiffusion and Immunoelectrophoresis the presence of ARS was determined in the blood serum of healthy persons as well as in those with higher enzyme activities. However the lack of ARS activity in blood serum was still in question. Further tests were conducted in order to answer this question using prepared hepatic cells. This cell suspension was obtained by perfusing rat liver with EDTA solution. These morphologically complete cells were then incubated in Krebs-Ringer solution. At certain incubation periods ARS activity was tested in extra-cellular fluid as well as in the cells. ARS activity as well as other enzyme activities (ASPAT, ALAT) were observed in extracellular fluid. This indicated that these enzymes exited the cells. Extra cellular activity of ARS was relatively low. Samples of ARS witii activities that were significantly higher than in the initial extracellular fluid were obtained from salted-out fractions. Simultaneously ARS activity was tested in complete, non-fractioned cell cytosol. It so happened that in this instance these enzymes had no activity. This indicated that perhaps the lack of ARS activity could be caused by some factor present in the cytosol as well as in blood serum that blocked their activity. The performance of fractioning of cytosol and blood serum showed that the fraction salted out by using over 70% ammonium sulphate was responsible for the process of ARS inactiva- tion. A closer analysis of this fraction showed that a protein with responsible for the inhibition function. This protein is present in both cytosol and blood serum and in both instances has similar quantities of amino acids. Aminoacylation is a two step and multicomponent reaction. Tests were conducted in order to determine the site where the aminoacylation inhibitor acted. These experiments showed that this inhibitor reacts with the ARS itself. It was also observed that the presence of strong protease inhibitors liquidates the inhibition effect of the tested protein. This fact, along with other observations, suggested that the ARS inhibitor which had been obtained may be a specific protease that damages the structure of these enzymes only. This idea is supported by knowledge of the fact that a natural ARS inhibitor is present in plants. The tests conducted below confirm that ARS is present in human blood serum as a result of passage from damaged tissues. They also confirmed their lack of activity in blood serum.

9

Influence of hyperthyroidism on acceptor activity of tRNA in some rabbit tissue

88%

Szymonik-Lesiuk S., Pasternak K., Brzuszkiewicz-Zarnowska H., Borkowski T.

Applied Biology Communications. Lublin Scientific Center

|

1993

|

tom 03

|

nr 1-2

10

An attempt at application of tRNA genes as promoters of protein-ciding genes in transgenic plants

88%

Kaczmarek W., Augustyniak J.

Acta Biochimica Polonica

|

1994

|

tom 41

|

nr 2

11

New intron-containing human tRNA Leu genes

88%

Karwowska U., Szweykowska-Kulinska Z.

Acta Biochimica Polonica

|

1997

|

tom 44

|

nr 4

Three new human nuclear tRNA(Leu) genes have been isolated and sequenced using the PCR technique. Two of them represent genes containing a CAA anticodon and both contain introns of 22 nucleotides in length but differing in sequence. Intron-containing prolongated anticodon stems can be folded into a secondary structure similar to that of yeast pre-tRNA(Leu). The evolutionary conserved secondary structure suggests the same role of intron sequences in the human and yeast pre-tRNA(Leu) maturation pathway.

12

Efektywnosc wiazania aminokwasow przez tRNA watroby narkotyzowanych myszy

75%

Pasternak K.

Medycyna Weterynaryjna

|

1996

|

tom 52

|

nr 12

786-787

The experiments were done on mice divided into three experimental and control groups. The test group of mice received morphine, ethanol or morphine plus ethanol. The control group received only 0.85% NaCl. tRNA was obtained by phenol extraction from the livers of tested and control mice. The quantity of often radioactive amino acids bound to tRNA was measured. Morphine and ethanol changed the quantity of amino acids bound to tRNA. It was different for an individual amino acid and for tested tRNAs.

13

Mini-tRNA jako narzedzie identyfikacji elementow struktury tRNA opowiedzialnych za aminoacylacje

75%

Bakowska K., Dudzinska-Bajorek B., Twardowski T.

Postępy Biochemii

|

2004

|

tom 50

|

nr 1

2-10

14

Modified tRNAs for probing tRNA binding sites on the ribosome

75%

Podkowinski J., Dymarek-Babs T., Gornicki P.

Acta Biochimica Polonica

|

1989

|

tom 36

|

nr 3-4

15

Selective binding of amino acids to yeast tRNA under high ionic strength conditions

75%

Stroinski A., Kedzierski W.

Roczniki Akademii Rolniczej w Poznaniu. Ogrodnictwo

|

1994

|

tom 22

71-77

16

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Purification of tobacco (Nicotiana tabacum L.) specific transfer ribonucleic acids. Partial nucleotide sequence of initiator tRNA

75%

Barciszewska M., Kaniewski W., Pietrzak M., Barciszewski J.

Prace Naukowe Instytutu Ochrony Roślin

|

1984

|

tom 26

|

nr 2

17

Specificity and mechanism of the cleavages induced in yeast tRNAPhe by magnesium ions

75%

Marciniec T., Ciesiolka J., Wrzesinski J., Wiewiorowski M., Krzyzosiak W. J.

Acta Biochimica Polonica

|

1989

|

tom 36

|

nr 3-4

18

Editing of plant mitochondrial transfer RNAs

75%

Fey J., Weil J. H., Tomita K., Cosset A., Dietrich A., Small I., Marechal-Drouard L.

Acta Biochimica Polonica

|

2001

|

tom 48

|

nr 2

Editing in plant mi to chon dria con sists in C to U changes and mainly af fects mes senger RNAs, thus pro vid ing the cor rect ge netic in for ma tion for the biosynthesis of mi to- chon drial (mt) pro teins. But ed it ing can also af fect some of the plant mt tRNAs encoded by the mt ge nome. In di cots, a C to U ed it ing event cor rects aC:A mis match into a U:A base-pair in the acceptor stem of mt tRNAPhe (GAA). In larch mitochondria, three C to U ed it ing events re store U: A base-pairs in the ac cep tor stem, D stem and anticodon stem, re spec tively, of mt tRNAHis (GUG). For both these mt tRNAs ed it ing of the pre cur sors is a pre req ui site for their pro cess ing into ma ture tRNAs. In po tato mt tRNACys (GCA), ed it ing con verts a C28:U42 mis match in the anticodon stem into a U28:U42 non-canonical base-pair, and reverse transcriptase minisequencing has shown that the mature mt tRNACys is fully edited. In the bryophyte Marchantia polymorpha this U res i due is en coded in the mt ge nome and evo lu tion ary stud ies sug gest that res to ra tion of the U28 res i due is nec es sary when it is not en coded in the gene. How ever, in vitro stud ies have shown that nei ther pro cess- ing of the pre cur sor nor amino acylation of tRNACys re quires C to U ed it ing at this po- si tion. But se quenc ing of the pu ri fied mt tRNACys has shown that Y is pres ent at po si tion 28, indicating that C to U editing is a prerequisite for the subsequent isomerization of U into Y at po si tion 28.

19

Mitochondrial tRNA in hyperthyroidism

75%

Pasternak K., Szymonik-Lesiuk S., Brzuszkiewicz-Zarnowska H., Borkowski T.

Acta Biochimica Polonica

|

1995

|

tom 42

|

nr 2

The mitochondrial tRNA were prepared from liver and brain tissues of thyroxinized and control rabbits. The presence of tRNA for twenty amino acids both in liver and brain mitochondria was revealed. The quantity of radioactive amino acids bound to the mitochondrial tRNA was higher in hyperthyreosis than in control animals but considerable differences between the brain and liver tissues were observed.

20

Activity of aminoacyl-tRNA synthetases in some tissues of thyroxinized rabbits

75%

Pasternak K., Szymonik-Lesiuk S., Brzuszkiewicz-Zarnowska H., Borkowski T.

Applied Biology Communications. Lublin Scientific Center

|

1994

|

tom 04

|

nr 3-4

Ograniczanie wyników

Probing the anticodon loop structure in yeast tRNAphey with single strand-specific nuclease S1

The activity of aminoacyl-tRNA synthetases in stomach cancer

Two intron-containing pre-tRNAsTyr from Triticum aestivum are efficiently processed and spliced in homologous cell-free extract

Is the tRNA ochre suppressor supX derived from gltT ?

Rapid separation of tyrosine - specific tRNA from white lupin

Nowo poznane funkcje transferowych kwasow rybonukleinowych i mozliwosci ich wykorzystania w biotechnologii

The response of the double strand-specific nuclease V1 to Y-base removal in yeast tRNA(Phe)

Pozakomórkowa obecność aminoacylo-tRNA syntetaz

Influence of hyperthyroidism on acceptor activity of tRNA in some rabbit tissue

An attempt at application of tRNA genes as promoters of protein-ciding genes in transgenic plants

New intron-containing human tRNA Leu genes

Efektywnosc wiazania aminokwasow przez tRNA watroby narkotyzowanych myszy

Mini-tRNA jako narzedzie identyfikacji elementow struktury tRNA opowiedzialnych za aminoacylacje

Modified tRNAs for probing tRNA binding sites on the ribosome

Selective binding of amino acids to yeast tRNA under high ionic strength conditions