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

2011 ◽  
Vol 75 (8) ◽  
pp. 1618-1620 ◽  
Author(s):  
Atsushi KONISHI ◽  
Daisuke NEMOTO ◽  
Kiyoshi YASUKAWA ◽  
Kuniyo INOUYE
Keyword(s):  
Reverse Transcriptase ◽  
Thermal Stabilities ◽  
Avian Myeloblastosis Virus ◽  
Α Subunit

Functional expression of the reverse transcriptase αβ heterodimer from avian myeloblastosis virus in Escherichia coli

2021 ◽  
Author(s):  
Yuriko Makino ◽  
Hiroshi Satoh ◽  
Atsushi Noguchi ◽  
Teruhiko Ide ◽  
Rie Yatsunami ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Reverse Transcriptase ◽  
Active Form ◽  
Functional Expression ◽  
Β Subunit ◽  
Rna Amplification ◽  
Avian Myeloblastosis Virus ◽  
Α Subunit ◽  
E Coli

Abstract The α subunit of avian myeloblastosis virus reverse transcriptase (AMV-RT) is generated from the β subunit by proteolysis, and the αβ heterodimer represents the active form. The codon optimized gene was expressed in E. coli, and an active αβ heterodimer was generated. The RNA amplification activity of the purified recombinant AMV-RT αβ heterodimer was similar to that of the native one.

scholarly journals Mn2+ Suppressor Mutations and Biochemical Communication between Ty1 Reverse Transcriptase and RNase H Domains

2007 ◽  
Vol 81 (17) ◽  
pp. 9004-9012 ◽  
Author(s):  
Robert M. Yarrington ◽  
Jichao Chen ◽  
Eric C. Bolton ◽  
Jef D. Boeke
Keyword(s):  
Reverse Transcriptase ◽  
Ion Homeostasis ◽  
Point Mutations ◽  
Rnase H ◽  
Avian Myeloblastosis Virus ◽  
Manganese Ion ◽  
Suppressor Mutations ◽  
Suppressor Mutants ◽  
Ty1 Retrotransposition

ABSTRACT Ty1 reverse transcriptase/RNase H (RT/RH) is exquisitely sensitive to manganese concentrations. Elevated intracellular free Mn2+ inhibits Ty1 retrotransposition and in vitro Ty1 RT-polymerizing activity. Furthermore, Mn2+ inhibition is not limited to the Ty1 RT, as this ion similarly inhibits the activities of both avian myeloblastosis virus and human immunodeficiency virus type 1 RTs. To further characterize Mn2+ inhibition, we generated RT/RH suppressor mutants capable of increased Ty1 transposition in pmr1Δ cells. PMR1 codes for a P-type ATPase that regulates intracellular calcium and manganese ion homeostasis, and pmr1 mutants accumulate elevated intracellular manganese levels and display 100-fold less transposition than PMR1 + cells. Mapping of these suppressor mutations revealed, surprisingly, that suppressor point mutations localize not to the RT itself but to the RH domain of the protein. Furthermore, Mn2+ inhibition of in vitro RT activity is greatly reduced in all the suppressor mutants, whereas RH activity and cleavage specificity remain largely unchanged. These intriguing results reveal that the effect of these suppressor mutations is transmitted to the polymerase domain and suggest biochemical communication between these two domains during reverse transcription.

scholarly journals Jnhibition of avian myeloblastosis virus reverse transcriptase by flavones and isoflavones.

1989 ◽  
Vol 42 (10) ◽  
pp. 1523-1525 ◽  
Author(s):  
YOSHIO INOUYE ◽  
KENJI YAMAGUCHI ◽  
YUKINORI TAKE ◽  
SHOSHIRO NAKAMURA
Keyword(s):  
Reverse Transcriptase ◽  
Avian Myeloblastosis Virus
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