Details

Autor(en) / Beteiligte

• Guo, Chao
• Han, Jingwen
• Liu, Yan
• Wang, Jinzhong
• Wang, Ying

Titel

Thermal stressed human immunodeficiency virus type 1 nucleocapsid protein NCp7 maintains nucleic acid-binding activity

Ist Teil von

• Biochemical and biophysical research communications, 2020-06, Vol.526 (3), p.721-727

Ort / Verlag

United States: Elsevier Inc

Erscheinungsjahr

2020

Link zum Volltext

Quelle

MEDLINE

Beschreibungen/Notizen

• The nucleocapsid protein (NC) of human immunodeficiency virus type 1 (HIV-1) is a small, highly basic nucleic acid (NA)-binding protein with two CCHC zinc-finger motifs. In this study, we report for the first time, to our knowledge, that thermal stressed HIV-1 NCp7 maintained NA-binding activity. About 41.3% of NCp7 remained soluble after incubated at 100 °C for 60 min, and heat-treated NCp7 maintained its abilities to bind to HIV-1 packaging signal (Psi) and the stem-loop 3 of the Psi. At high or very high degrees of sequence occupancy, NCp7 inhibited first-strand cDNA synthesis catalyzed by purified HIV-1 reverse transcriptase, and heat-treated NCp7 maintained the inhibition. Moreover, both EDTA-treated and H23K + H44K double mutant of NCp7 inhibited first-strand cDNA synthesis, demonstrating that the NA-binding activity of NCp7 at high NC:NA ratios is independent on its zinc-fingers. These results may benefit further investigations of the structural stability and function of NCp7 in viral replication. •About 41.3% of NCp7 remained soluble after incubated at 100 °C for 60 min.•Heat-treated NCp7 maintained Psi and SL3-RNA binding activities.•At high NC:NA ratios, NCp7 inhibited first-strand cDNA synthesis.•Heat-treated NCp7 still inhibited first-strand cDNA synthesis.•NA-binding activity of NCp7 at high NC:NA ratios is independent on zinc-fingers.