Статья

The attachment of a DNA-binding Sso7d-like protein improves processivity and resistance to inhibitors of M-MuLV reverse transcriptase

I. Oscorbin, P. Wong, U. Boyarskikh, E. Khrapov, M. Filipenko,
2020

Reverse transcriptases (RTs) are a standard tool in both fundamental studies and diagnostics. RTs should possess elevated temperature optimum, high thermal stability, processivity and tolerance to contaminants. Here, we constructed a set of chimeric RTs, based on the combination of the Moloney murine leukaemia virus (M-MuLV) RT and either of two DNA-binding domains: the DNA-binding domain of the DNA ligase from Pyrococcus abyssi or the DNA-binding Sto7d protein from Sulfolobus tokodaii. The processivity and efficiency of cDNA synthesis of the chimeric RT with Sto7d at the C-end are increased several fold. The attachment of Sto7d enhances the tolerance of M-MuLV RT to the most common amplification inhibitors: NaCl, urea, guanidinium chloride, formamide, components of human whole blood and human blood plasma. Thus, fusing M-MuLV RT with an additional domain results in more robust and efficient RTs.

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Версии

  • 1. Version of Record от 2020-12-01

Метаданные

Об авторах
  • I. Oscorbin
    Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk State University
  • P. Wong
    Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk State University
  • U. Boyarskikh
    Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk State University
  • E. Khrapov
    Institute of Chemical Biology and Fundamental Medicine, SB RAS
  • M. Filipenko
    Institute of Chemical Biology and Fundamental Medicine, SB RAS, Novosibirsk State University
Название журнала
  • FEBS Letters
Том
  • 594
Выпуск
  • 24
Страницы
  • 4338-4356
Финансирующая организация
  • Russian Science Foundation
Номер гранта
  • undefined
Тип документа
  • journal article
Тип лицензии Creative Commons
  • CC BY
Правовой статус документа
  • Свободная лицензия
Источник
  • scopus