The C-terminal domain of glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNA^Lys3 packaging into human immunodeficiency virus type-1 particles.

ABSTRACT: Human immunodeficiency virus type-1 (HIV-1) requires the packaging of human tRNA^Lys3 as a primer for effective viral reverse transcription. Previously, we reported that glyceraldehyde 3-phosphate dehydrogenase (GAPDH) suppresses the packaging efficiency of tRNA^Lys3. Although the binding of GAPDH to Pr55 ^gag is important for the suppression mechanism, it remains unclear which domain of GAPDH is responsible for the interaction with Pr55 ^gag . In this study, we show that Asp²⁵⁶, Lys²⁶⁰, Lys²⁶³ and Glu²⁶⁷ of GAPDH are important for the suppression of tRNA^Lys3 packaging. Yeast two-hybrid analysis demonstrated that the C-terminal domain of GAPDH (151-335) interacts with both th

SUBMITTER: Kishimoto N 

PROVIDER: S-EPMC5614461 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature