Related Experiment Video

Updated: Feb 15, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
08:16

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays

Published on: December 29, 2021

3.3K

The central domain of UNC-45 chaperone inhibits the myosin power stroke

Paul J Bujalowski1, Paul Nicholls2, Eleno Garza3

  • 1Department of Biochemistry and Molecular Biology The University of Texas Medical Branch Galveston TX USA.

FEBS Open Bio
|January 12, 2018
PubMed

Insights

The UNC-45B chaperone

Area of Science:

  • Muscle biology and protein folding.

Background:

  • UNC-45B is a crucial chaperone for sarcomeric myosin.
  • Its TPR and UCS domains' functions are known, but the central domain's role is unclear.

Purpose of the Study:

  • To elucidate the function of the UNC-45B central domain.
  • To understand its role in myosin motor activity and actin translocation.

Main Methods:

  • Utilized in vitro myosin motility assays.
  • Employed ATPase assays to study myosin function.

Main Results:

  • The central domain of UNC-45B alone inhibits the myosin power stroke.
  • This inhibition occurs via a mechanism allowing ATP turnover.
  • UNC-45B's domains have distinct roles: TPR recruits Hsp90, UCS has chaperone activity, and the central domain inhibits myosin's actin translocation.

Conclusions:

  • UNC-45B's central domain is a novel inhibitor of myosin's actin translocation function.
  • This inhibitory role is hypothesized to be important in myofibril assembly and sarcomere development, especially under stress.
Keywords:
UNC‐45chaperonemyosin

More Related Videos

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions06:55

Using Caenorhabditis elegans to Screen for Tissue-Specific Chaperone Interactions

Published on: June 7, 2020

3.4K
Autoradiographic Measurements of [14C]-Iodoantipyrine in Rat Brain Following Central Post-Stroke Pain07:27

Autoradiographic Measurements of [14C]-Iodoantipyrine in Rat Brain Following Central Post-Stroke Pain

Published on: July 18, 2016

9.2K

Related Concept Videos

Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
20.0K
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

15.1K
Feedback Inhibition00:46

Feedback Inhibition

Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
57.4K
Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to...
14.7K
The Central Dogma01:25

The Central Dogma

Overview
140.1K
Actin and Myosin in Muscle Contraction01:16

Actin and Myosin in Muscle Contraction

Actin and myosin are contractile proteins that form the sarcomere found in skeletal muscle tissues for regulating muscle contraction. Actin, a globular contractile protein, interacts with myosin for muscle contraction. The skeletal tissue appears striped or striated under a microscope due to the repeated arrangement of contractile proteins actin and myosin along the length of myofibrils. Dark A bands and light I bands repeat along myofibrils, and the alignment of myofibrils in the cell causes...
24.7K