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Titolo:
Effect of tetrahydropyrimidine derivatives on protein nucleic acids interaction - Type II restriction endonucleases as a model system
Autore:
Malin, G; Iakobashvili, R; Lapidot, A;
Indirizzi:
Weizmann Inst Sci, Dept Organ Chem, IL-76100 Rehovot, Israel Weizmann InstSci Rehovot Israel IL-76100 Chem, IL-76100 Rehovot, Israel
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 11, volume: 274, anno: 1999,
pagine: 6920 - 6929
SICI:
0021-9258(19990312)274:11<6920:EOTDOP>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
CHROMATOGRAPHY-MASS-SPECTROMETRY; PRODUCER STREPTOMYCES-PARVULUS; ECO-RI ENDONUCLEASE; ESCHERICHIA-COLI; CORYNEBACTERIUM-GLUTAMICUM; HALOPHILIC EUBACTERIA; COMPATIBLE SOLUTES; MAGNETIC-RESONANCE; DNA RECOGNITION; STRESS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
59
Recensione:
Indirizzi per estratti:
Indirizzo: Lapidot, A Weizmann Inst Sci, Dept Organ Chem, IL-76100 Rehovot, Israel Weizmann Inst Sci Rehovot Israel IL-76100 100 Rehovot, Israel
Citazione:
G. Malin et al., "Effect of tetrahydropyrimidine derivatives on protein nucleic acids interaction - Type II restriction endonucleases as a model system", J BIOL CHEM, 274(11), 1999, pp. 6920-6929

Abstract

2-Methyl-4-carboxy,5-hydroxy-3,4,5,6-tetrahydropyrimidine (THP(A) or hydroxyectoine) and 2-methyl,4-carboxy-3, 4,5,6-tetrahydropyrimidine (THP(B) or ectoine) are now recognized as ubiquitous bacterial osmoprotectants, To evaluate the impact of tetrahydropyrimidine derivatives (THPs) on protein-DNA interaction and on restriction-modification systems, we have examined theireffect on the cleavage of plasmid DNA by 10 type II restriction endonucleases. THP(A) completely arrested the cleavage of plasmid and bacteriophage ADNA by EcoRI endonuclease at 0.4 mM and the oligonucleotide (d(CGCGAATTCGCG))(2) at about 4.0 mM. THP(B) was 10-fold less effective than THP(A), whereas for betaine and proline, a notable inhibition was observed only at 100 mM, Similar effects of THP(A) were observed for all tested restriction endonucleases, except for SmaI and PvuII, which were inhibited only partially at 50 mM THP(A), No effect of THP(A) on the activity of DNase I, RNase A, and Tag DNA polymerase was noticed. Gel-shift assays showed that THP(A) inhibited the EcoRI-(d-(CGCGAATTCGCG))(2) complex formation, whereas facilitateddiffusion of EcoRI along the DNA was not affected. Methylation of the carboxy group significantly decreased the activity of THPs, suggesting that their zwitterionic character is essential for the inhibition effect. Possible mechanisms of inhibition, the role of THPs in the modulation of the protein-DNA interaction, and the in vivo relevance of the observed phenomena are discussed.

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Documento generato il 29/11/20 alle ore 03:16:02