Skip to main content
placeholder image

Using single-molecule approaches to understand the molecular mechanisms of heat-shock protein chaperone function

Journal Article


Download full-text (Open Access)

Abstract


  • The heat-shock proteins (Hsp) are a family of molecular chaperones, which collectively form a network that is critical for the maintenance of protein homeostasis. Traditional ensemble-based measurements have provided a wealth of knowledge on the function of individual Hsps and the Hsp network; however, such techniques are limited in their ability to resolve the heterogeneous, dynamic and transient interactions that molecular chaperones make with their client proteins. Single-molecule techniques have emerged as a powerful tool to study dynamic biological systems, as they enable rare and transient populations to be identified that would usually be masked in ensemble measurements. Thus, single-molecule techniques are particularly amenable for the study of Hsps and have begun to be used to reveal novel mechanistic details of their function. In this review, we discuss the current understanding of the chaperone action of Hsps and how gaps in the field can be addressed using single-molecule methods. Specifically, this review focuses on the ATP-independent small Hsps and the broader Hsp network and describes how these dynamic systems are amenable to single-molecule techniques.

Publication Date


  • 2018

Citation


  • Johnston, C. L., Marzano, N. R., van Oijen, A. M. & Ecroyd, H. (2018). Using Single-Molecule Approaches to Understand the Molecular Mechanisms of Heat-Shock Protein Chaperone Function. American Journal of Molecular Biology, 430 (22), 4525-4546.

Scopus Eid


  • 2-s2.0-85048515745

Ro Full-text Url


  • https://ro.uow.edu.au/cgi/viewcontent.cgi?article=1308&context=smhpapers1

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/304

Number Of Pages


  • 21

Start Page


  • 4525

End Page


  • 4546

Volume


  • 430

Issue


  • 22

Place Of Publication


  • United States

Abstract


  • The heat-shock proteins (Hsp) are a family of molecular chaperones, which collectively form a network that is critical for the maintenance of protein homeostasis. Traditional ensemble-based measurements have provided a wealth of knowledge on the function of individual Hsps and the Hsp network; however, such techniques are limited in their ability to resolve the heterogeneous, dynamic and transient interactions that molecular chaperones make with their client proteins. Single-molecule techniques have emerged as a powerful tool to study dynamic biological systems, as they enable rare and transient populations to be identified that would usually be masked in ensemble measurements. Thus, single-molecule techniques are particularly amenable for the study of Hsps and have begun to be used to reveal novel mechanistic details of their function. In this review, we discuss the current understanding of the chaperone action of Hsps and how gaps in the field can be addressed using single-molecule methods. Specifically, this review focuses on the ATP-independent small Hsps and the broader Hsp network and describes how these dynamic systems are amenable to single-molecule techniques.

Publication Date


  • 2018

Citation


  • Johnston, C. L., Marzano, N. R., van Oijen, A. M. & Ecroyd, H. (2018). Using Single-Molecule Approaches to Understand the Molecular Mechanisms of Heat-Shock Protein Chaperone Function. American Journal of Molecular Biology, 430 (22), 4525-4546.

Scopus Eid


  • 2-s2.0-85048515745

Ro Full-text Url


  • https://ro.uow.edu.au/cgi/viewcontent.cgi?article=1308&context=smhpapers1

Ro Metadata Url


  • http://ro.uow.edu.au/smhpapers1/304

Number Of Pages


  • 21

Start Page


  • 4525

End Page


  • 4546

Volume


  • 430

Issue


  • 22

Place Of Publication


  • United States