Comparison of the Thermal Stabilities of the αβ Heterodimer and the α Subunit of Avian Myeloblastosis Virus Reverse Transcriptase | Zendy

Atsushi Konishi | Zendy; Daisuke Nemoto | Zendy; Kiyoshi Yasukawa | Zendy; Kuniyo Inouye | Zendy

Open Access

Comparison of the Thermal Stabilities of the αβ Heterodimer and the α Subunit of Avian Myeloblastosis Virus Reverse Transcriptase

Author(s) -

Atsushi Konishi,

Daisuke Nemoto,

Kiyoshi Yasukawa,

Kuniyo Inouye

Publication year - 2011

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.110238

Subject(s) - protein subunit , reverse transcriptase , recombinant dna , virology , primer (cosmetics) , microbiology and biotechnology , chemistry , virus , biology , biochemistry , polymerase chain reaction , gene , organic chemistry

Avian myeloblastosis virus reverse transcriptase (AMV RT) is a heterodimer consisting of a 63-kDa α subunit and a 95-kDa β subunit. In this study, we explored the role of the interaction between the α and β subunits on AMV RT stability. The recombinant AMV RT α subunit was expressed in insect cells and purified. It exhibited lower thermal stability than the native AMV RT αβ heterodimer. Unlike the αβ heterodimer, the α subunit was not stabilized by template-primer. These results suggest that interaction between the α and β subunits is important for AMV RT stability.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research