JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2022  1,200
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 45(2011) N 5 p. 833-842;
V.A. Chernikov1*, N.V. Gorokhovets2, L.V. Savvateeva2, S.E. Severin1**

Functional Characterization of Recombinant Human HSP70 Domains and Interdomain Interactions

1Moscow Research Institute of Medical Ecology, Moscow, 117149, Russia
2Research Institute of Molecular Medicine, Sechenov Moscow Medical Academy, Moscow, 119991, Russia

*v_scherrry@mail.ru
**sergsev@aha.ru
Received - 2010-09-06; Accepted - 2011-02-17

ATPase and peptide-binding activity of recombinant human heat shock proteins HSP70A1B and HSC70 and two hybrid proteins derived from them was investigated. UV-spectral recorded data were used to characterize conformational rearrangements induced by domain replacement or HSP70-peptide interaction. It was shown that the N-terminal domain dramatically affects the substrate specificity of the C-terminal peptidebinding domain, which puts forward a new hypothesis for HSP70 chaperone machinery. On the other hand, the peptide-binding domain affected the ATPase activity of the recombinant proteins. There was a linear relationship between the ATPase activity and the peptide complex percentage. This connection can be used for quantification of HSP70 complexes with unlabeled peptides.

heat shock protein, interdomain interaction, ATPase activity, UV-spectral analysis



JMB-FOOTER RAS-JOURNALS