The C-terminal domain of glyceraldehyde 3-phosphate dehydrogenase plays an important role in suppression of tRNALys3 packaging into human immunodeficiency virus type-1 particles
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- 作者：Naoki Kishimotoa ; Ayano Onitsuka-Kishimotoa ; Nozomi Igaa ; Nobutoki Takamuneb ; Shozo Shojia ; Shogo Misumia ; misumi@gpo.kumamoto-u.ac.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：GAPDH ; glyceraldehyde 3-phosphate dehydrogenase ; HIV-1 ; human immunodeficiency virus type 1 ; LysRS ; lysyl-tRNA synthetase ; MA ; matrix ; CA ; capsid
- 刊名：Biochemistry and Biophysics Reports
- 出版年：2016
- 出版时间：December 2016
- 年：2016
- 卷：8
- 期：Complete
- 页码：325-332
- 全文大小：1157 K
文摘
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Yeast two-hybrid analysis revealed that GAPDH interacts with MA and CA region of HIV-1 precursor proteins via its C-terminal domain.
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Docking simulation predicted that GAPDH helix 10, which is exposed on surface of its tetrameric form surface, interacts with MA and CA.
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Mutagenesis assay on yeast two-hybrid analysis showed that D256R/K260E/K263E/E267R mutant of GAPDH lacks the binding affinity to both MA and CA.
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D256R/K260E/K263E/E267R mutant of GAPDH acts as dominant negative effector on the packaging of tRNALys3.