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Here, we constructed a set of chimeric RTs, based on the combination of the Moloney murine leukaemia virus (M\u2010MuLV) RT and either of two DNA\u2010binding domains: the DNA\u2010binding domain of the DNA ligase from\n                    <jats:italic>Pyrococcus\u00a0abyssi<\/jats:italic>\n                    or the DNA\u2010binding Sto7d protein from\n                    <jats:italic>Sulfolobus\u00a0tokodaii<\/jats:italic>\n                    . The processivity and efficiency of cDNA synthesis of the chimeric RT with Sto7d at the C\u2010end are increased several fold. The attachment of Sto7d enhances the tolerance of M\u2010MuLV RT to the most common amplification inhibitors: NaCl, urea, guanidinium chloride, formamide, components of human whole blood and human blood plasma. Thus, fusing M\u2010MuLV RT with an additional domain results in more robust and efficient RTs.\n                  <\/jats:p>","DOI":"10.1002\/1873-3468.13934","type":"journal-article","created":{"date-parts":[[2020,9,24]],"date-time":"2020-09-24T14:49:00Z","timestamp":1600958940000},"page":"4338-4356","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":24,"title":["The attachment of a DNA\u2010binding Sso7d\u2010like protein improves processivity and resistance to inhibitors of M\u2010MuLV reverse transcriptase"],"prefix":"10.1002","volume":"594","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-3754-5824","authenticated-orcid":false,"given":"Igor P.","family":"Oscorbin","sequence":"first","affiliation":[{"name":"Institute of Chemical Biology and Fundamental Medicine Siberian Branch of the Russian Academy of Sciences Novosibirsk Russia"},{"name":"Novosibirsk State University Novosibirsk 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