Replacement of Arg in the conserved N-terminal RLFDQxFG motif affects physico-chemical properties and chaperone-like activity of human small heat shock protein HspB8 (Hsp22).
The small heat shock protein (sHsp) called HspB8 (formerly, Hsp22) is one of the least typical sHsp members, whose oligomerization status remains debatable. Here we analyze the effect of mutations in a highly conservative sequence located in the N-terminal domain of human HspB8 on its physico-chemic...
Main Authors: | Vladislav M Shatov, Nikolai N Sluchanko, Nikolai B Gusev |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2021-01-01
|
Series: | PLoS ONE |
Online Access: | https://doi.org/10.1371/journal.pone.0253432 |
Similar Items
-
The Role of the Arginine in the Conserved N-Terminal Domain RLFDQxFG Motif of Human Small Heat Shock Proteins HspB1, HspB4, HspB5, HspB6, and HspB8
by: Vladislav M. Shatov, et al.
Published: (2018-07-01) -
Quaternary Structure and Hetero-Oligomerization of Recombinant Human Small Heat Shock Protein HspB7 (cvHsp)
by: Lydia K. Muranova, et al.
Published: (2021-07-01) -
HspB1, HspB5 and HspB4 in Human Cancers: Potent Oncogenic Role of Some of Their Client Proteins
by: André-Patrick Arrigo, et al.
Published: (2014-02-01) -
The chaperone HSPB1 prepares protein aggregates for resolubilization by HSP70
by: Conrado C. Gonçalves, et al.
Published: (2021-08-01) -
Characterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron Diseases.
by: Lydia K Muranova, et al.
Published: (2015-01-01)