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首页> 外文期刊>New biotechnology >Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules
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Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules

机译：通过定点聚乙二醇化使M-MuLV RT RNase H活性选择性失活：提高了合成长cDNA分子的能力

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摘要

Moloney murine leukemia virus reverse transcriptase (M-MuLV RT) is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules. Here we present the PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity. We demonstrate that sitedirected chemical modification (SDCM) of the RNase H domain by selectively PEGylating C635, one of the eight cysteine residues present in the reverse transcriptase (RT), specifically inactivated its ribonucleolytic activity. As a consequence, the efficiency of long cDNA molecules synthesis by modified enzyme was greatly increased.
机译：莫洛尼氏鼠白血病病毒逆转录酶（M-MuLV RT）是一种域结构化酶，具有N端位于DNA聚合活性和C端位于RNase H的活性，这会干扰长cDNA分子的有效合成。在这里，我们介绍了PEG化作为工程化RNase H活性不足的M-MuLV RT衍生物的工具。我们证明了通过选择性地PEG化C635，逆转录酶（RT）中存在的八个半胱氨酸残基之一，对RNase H结构域进行定点化学修饰（SDCM），特别是使其失活。结果，大大提高了通过修饰酶合成长cDNA分子的效率。

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