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Biochemical and biophysical research communications, 2017-12, Vol.494 (1-2), p.57-62
2017
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Autor(en) / Beteiligte
Titel
Ubiquitination of non-lysine residues in the retroviral integrase
Ist Teil von
  • Biochemical and biophysical research communications, 2017-12, Vol.494 (1-2), p.57-62
Ort / Verlag
United States: Elsevier Inc
Erscheinungsjahr
2017
Quelle
ScienceDirect
Beschreibungen/Notizen
  • Retroviral integrase catalyzes the integration of retroviral genome into host chromosomal DNA, which is a prerequisite of effective viral replication and infection. The human immunodeficiency virus type 1 (HIV-1) integrase has previously been reported to be regulated by the ubiquitination, but the molecular characterization of integrase ubiquitination is still unclear. In this study, we analyzed the ubiquitination of avian leukosis virus (ALV) integrase in detail. The ubiquitination assay showed that, like HIV-1, ALV integrase could also be modified by ubiquitination when expressed in 293 T and DF-1 cells. Domain mapping analysis revealed that the ubiquitination of ALV integrase might mainly occurred in the catalytic core and the N-terminal zinc-binding domains. Both lysine and non-lysine residues within integrase of ALV and HIV-1 were responsible for the ubiquitin conjugation, and the N-terminal HHCC zinc-binding motif might play an important role in mediating integrase ubiquitination. Interestingly, mass spectrometry analysis identified the Thr10 and Cys37 residues in the HHCC zinc-binding motif as the ubiquitination sites, indicating that ubiquitin may be conjugated to ALV integrase through direct interaction with the non-lysine residues. These findings revealed the detailed features of retroviral integrase ubiquitination and found a novel mechanism of ubiquitination mediated by the non-lysine residues within the N-terminal zinc-binding domain of integrase. •Integrases of ALV and HIV-1 are modified by ubiquitination.•Both lysine and non-lysine residues within integrases of ALV and HIV-1 are responsible for the ubiquitin conjugation.•The N-terminal HHCC zinc-binding motif is critical for mediating ubiquitination of ALV integrase.•Thr10 and Cys37 in the N-terminal zinc-binding motif are identified as the ubiquitination sites of ALV integrase.

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