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Chaperone-Like Activity of HSPB5: The Effects of Quaternary Structure Dynamics and Crowding
- Source :
- International Journal of Molecular Sciences, Volume 21, Issue 14, International Journal of Molecular Sciences, Vol 21, Iss 4940, p 4940 (2020)
- Publication Year :
- 2020
- Publisher :
- Multidisciplinary Digital Publishing Institute, 2020.
-
Abstract
- Small heat-shock proteins (sHSPs) are ATP-independent molecular chaperones that interact with partially unfolded proteins, preventing their aberrant aggregation, thereby exhibiting a chaperone-like activity. Dynamics of the quaternary structure plays an important role in the chaperone-like activity of sHSPs. However, relationship between the dynamic structure of sHSPs and their chaperone-like activity remains insufficiently characterized. Many factors (temperature, ions, a target protein, crowding etc.) affect the structure and activity of sHSPs. The least studied is an effect of crowding on sHSPs activity. In this work the chaperone-like activity of HSPB5 was quantitatively characterized by dynamic light scattering using two test systems, namely test systems based on heat-induced aggregation of muscle glycogen phosphorylase b (Phb) at 48 &deg<br />C and dithiothreitol-induced aggregation of &alpha<br />lactalbumin at 37 &deg<br />C. Analytical ultracentrifugation was used to control the oligomeric state of HSPB5 and target proteins. The possible anti-aggregation functioning of suboligomeric forms of HSPB5 is discussed. The effect of crowding on HSPB5 anti-aggregation activity was characterized using Phb as a target protein. The duration of the nucleation stage was shown to decrease with simultaneous increase in the relative rate of aggregation of Phb in the presence of HSPB5 under crowded conditions. Crowding may subtly modulate sHSPs activity.
- Subjects :
- Models, Molecular
0301 basic medicine
Protein Conformation
Glycogen phosphorylase B
Article
Catalysis
chaperone-like activity
Inorganic Chemistry
lcsh:Chemistry
Protein Aggregates
Structure-Activity Relationship
03 medical and health sciences
Dynamic light scattering
Prohibitins
Protein Interaction Mapping
Chemical Precipitation
Humans
Physical and Theoretical Chemistry
Molecular Biology
lcsh:QH301-705.5
Spectroscopy
mixed crowding
oligomeric states
030102 biochemistry & molecular biology
biology
Chemistry
HSPB5
Organic Chemistry
Temperature
alpha-Crystallin B Chain
General Medicine
Crowding
Dynamic Light Scattering
Recombinant Proteins
Computer Science Applications
Dithiothreitol
Kinetics
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Chaperone (protein)
Lactalbumin
biology.protein
Biophysics
Glycogen Phosphorylase, Muscle Form
Protein quaternary structure
Target protein
Ultracentrifugation
Subjects
Details
- Language :
- English
- ISSN :
- 14220067
- Database :
- OpenAIRE
- Journal :
- International Journal of Molecular Sciences
- Accession number :
- edsair.doi.dedup.....66382acc356b3077037f0a3443414a3e
- Full Text :
- https://doi.org/10.3390/ijms21144940