Comparison of the Thermal Stabilities of the αβ Heterodimer and the α Subunit of Avian Myeloblastosis Virus Reverse Transcriptase
Comparison of the Thermal Stabilities of the αβ Heterodimer and the α Subunit of Avian Myeloblastosis Virus Reverse Transcriptase
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DOI：
10.1271/bbb.110238
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发表时间：
2011-08-01
影响因子：
1.6
通讯作者：
Inouye, Kuniyo
中科院分区：
文献类型：
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作者：
Konishi, Atsushi;Nemoto, Daisuke;Inouye, Kuniyo
禽成髓细胞瘤病毒逆转录酶（AMV RT）是由63-kDa α亚基和95-kDa β亚基组成的异源二聚体。在这项研究中，我们探讨了AMV RT稳定性的α和β亚基之间的相互作用的作用。重组AMV RT α亚基在昆虫细胞中表达并纯化。它表现出比天然AMV RT α β异二聚体更低的热稳定性。与α β异二聚体不同，α亚基不被模板-引物稳定。这些结果表明α和β亚基之间的相互作用对于AMV RT稳定性是重要的。
Avian myeloblastosis virus reverse transcriptase (AMV RT) is a heterodimer consisting of a 63-kDa alpha subunit and a 95-kDa beta subunit. In this study, we explored the role of the interaction between the a and beta subunits on AMV RT stability. The recombinant AMV RT alpha subunit was expressed in insect cells and purified. It exhibited lower thermal stability than the native AMV RT alpha beta heterodimer. Unlike the alpha beta heterodimer, the alpha subunit was not stabilized by template-primer. These results suggest that interaction between the alpha and beta subunits is important for AMV RT stability.