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Oligonucleotide cleavage by restriction endonucleases MvaI and EcoRII: a comprehensive study on the influence of structural parameters on the enzyme-substrate interactionстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: Kubareva E.A., Gromova E.S., Pein С.D., Krug A., Oretskaya T.S., Cech D., Shabarova Z.A.
- Журнал: Biochimica et Biophysica Acta - Proteins and Proteomics
- Том: 1088
- Номер: 3
- Год издания: 1991
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 395
- Последняя страница: 400
- DOI: 10.1016/0167-4781(91)90131-5
- Аннотация: To elucidate the mechanism of action of the restriction endonucleases - isoschizomers Eco RII and MvaI - a study was made of their interaction with a set of synthetic oligonucleotide duplexes containing a single 5'-d(CC(A)/(T)GG)-3' Eco RII (MvaI) recognition site. The substrates had varying length and structure of the nucleotide sequences flanking the recognition site. The structure of the flanking sequence is important for the cleavage by Eco RII and MvaI enzymes; there is a structure which was found to speed up the Eco RII and MvaI action. The cleavage of oligonucleotide duplexes by Eco RII enzyme does not go to completion. Eco RII endonuclease cleaved extended substrates less efficiently than short ones. Extension of the flanking sequences, with the same nucleotide surrounding of the recognition site, substantially altered the whole kinetic pattern of MvaI hydrolysis. This was not observed with Eco RII enzyme. The restriction endonuclease MvaI distinguished between dA and dT residues in the recognition site, which was reflected in the higher rate of hydrolysis of the dA-containing strand of the quasipalindromic DNA duplex.
- Добавил в систему: Орецкая Татьяна Семеновна