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Chemical Ribonucleases: 4.1 An Analysis of the Domain Structure of Chemical Ribonucleases Based on 1,4-Diazabicyclo[2.2.2]octane Full article

Общее Language: Английский, Genre: Full article,
Status: Published, Source type: Translated
Journal Russian Journal of Bioorganic Chemistry
ISSN: 1068-1620 , E-ISSN: 1608-330X
Output data Year: 2002, Volume: 28, Number: 4, Pages: 331-341 Pages count : 11 DOI: 10.1023/A:1019504227151
Tags Artificial ribonucleases, Domain structure, RNA, hydrolysis
Authors Konevetz D.A. 1 , Mironova N.L. 2 , Beck I.E. 3 , Zenkova M.A. 1 , Shishkin G.V. 1 , Vlassov V.V. 1 , Silnikov V.N. 1
Affiliations
1 Novosibirsk Institute of Bioorganic Chemistry, Russian Academy of Sciences, Siberian Branch, pr. Akademika Lavrent’eva 8, Novosibirsk, 630090 Russia
2 Novosibirsk State University, ul. Pirogova 2, Novosibirsk, 630090 Russia
3 Boreskov Institute of Catalysis, Russian Academy of Sciences, Siberian Branch, pr. Akademika Lavrent’eva 5, Novosibirsk, 630090 Russia

Funding (5)

1 Russian Foundation for Basic Research 00-15-97969
2 Russian Foundation for Basic Research 99-04-49538
3 Wellcome Trust 063630
4 The Ministry of Education and Science of the Russian Federation
5 Президиум РАН 219

Abstract: Artificial ribonucleases of the ABLkCm series were synthesized. They consist of a lipophilic alkyl radical (Et, n-C14H29, or n-C15H31) Ä, an “RNA-binding domain” Ç (bisquaternary salt of 1,4-diazabicyclo[2.2.2]octane), a “catalytic domain” ëm [histamine (ë1) or histidine (ë3) residue], and a “linker” Lk that joins the “domains” B and Cm [here, k is the number of methylene units (one or three) in the linker]. The effect of the “domain structure” on the catalytic properties of the chemical ribonucleases was analyzed using seven compounds of this series (ABL1C1, ABL3C1, ABL3C3, AC1, AB, BL2, and BL3C3). The catalytic activity of the compounds was assessed in the reaction of hydrolysis of the in vitro transcripts of human tRNALys and yeast tRNAAsp under physiological conditions. It was shown that only chemical ribonucleases that involve all the fragments of the ABLkCm construct can hydrolyze the substrate tRNA at a high rate (90% of tRNA is hydrolyzed for 10 h at 37°ë). The activity of the compounds is largely determined by the presence of a long lipophilic radical linked to 1,4-diazabicyclo[2.2.2]octane and a long linker, which joins the RNA-hydrolyzing and RNA-binding domains. The results indicate an important role of hydrophobic interactions in the acceleration of the RNA hydrolysis reaction.
Cite: Konevetz D.A. , Mironova N.L. , Beck I.E. , Zenkova M.A. , Shishkin G.V. , Vlassov V.V. , Silnikov V.N.
Chemical Ribonucleases: 4.1 An Analysis of the Domain Structure of Chemical Ribonucleases Based on 1,4-Diazabicyclo[2.2.2]octane
Russian Journal of Bioorganic Chemistry. 2002. V.28. N4. P.331-341. DOI: 10.1023/A:1019504227151 publication_identifier_short.wos_identifier_type publication_identifier_short.scopus_identifier_type publication_identifier_short.rinz_identifier_type
ArticleLinkType.TRANSLATED_TO_ORIGINAL: Коневец Д.А. , Миронова Н.Л. , Бекк И.Э. , Зенкова М.А. , Шишкин Г.В. , Власов В.В. , Сильников В.Н.
Химические рибонуклеазы. 4. Анализ фрагментной структуры химических рибонуклеаз на основе 1,4-диазабицикло[2.2.2]октана
Биоорганическая химия. 2002. Т.28. №4. С.367-378. publication_identifier_short.scopus_identifier_type publication_identifier_short.rinz_identifier_type
Dates:
Submitted: May 14, 2001
Published print: Jul 1, 2002
Identifiers:
publication_identifier.wos_identifier_type WOS:000177708000013
publication_identifier.scopus_identifier_type 2-s2.0-0036340955
publication_identifier.rinz_identifier_type 13400305
publication_identifier.accession_number_identifier_type 2002:575812
publication_identifier.chemical_accession_number_identifier_type 137:381573
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