Study on PrP106-126 peptide disturbed dimeration of 14-3-3β
10.3760/cma.j.issn.1003-9279.2013.02.009
- VernacularTitle:PrP106-126多肽抑制14-3-3β蛋白二聚体形成的研究
- Author:
Qin-Qin SONG
1
;
Peng SUN
;
Juan SONG
;
Lin-Jun SHENG
;
Jin ZHANG
;
Jun HAN
Author Information
1. 中国疾病预防控制中心病毒病预防控制所传染病预防控制所国家重点实验室
- Keywords:
Protein engineering;
Peptides;
Dimerization
- From:
Chinese Journal of Experimental and Clinical Virology
2013;27(2):109-111
- CountryChina
- Language:Chinese
-
Abstract:
Objective To investigate both PrP and PrP106-126 peptide effect on 14-3-3β dimeration.Methods 14-3-3β were incubated with different does recombinant PrP or PrP106-126 peptide,both 14-3-3β dimer and polymer were separated 15％ non-denaturing polyacrylamide gel electrophoresis (PAGE) and the 14-3-3 dimers were evaluated using 14-3-3β-specific Western blotting.And then,14-3-3β dimeration buffer were incubated with different does recombinant PrP and 250 μmol/L PrP106-126 peptide,14-3-3β dimer and polymer were detected by above methods.Cellular 14-3-3 dimer were also detected after PrP106-126 peptide were added to HeLa cell for 8 hours.Results Recombinant full-length PrP facilitated the dimerization of 14-3-3β and PrP106-126 disturbed 14-3-3β dimeration as both have dose dependence effect.PrP antagonized PrP106-126-induced 14-3-3β dimer with PrP protein increase in vitro.Cellular 14-3-3 dimerization also decreased after treatment of peptide PrP106-126 on HeLa cells for 8 hours.Conculsion Dimerization process of 14-3-3β was promoted by full-length PrP (PrP23-231) but inhibited by peptide PrP106-126 in vitro.PrP agonized PrP106-126-induced inhibition of 14-3-3 dimeration.PrP106-126 inhibited cellular 14-3-3 dimerization.
