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      Life under tension: the relevance of force on biological polymers

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      Author(s): 1 , 2 , * , , 1
      Publication date (Print):
      Journal: Biophysics Reports
      Publisher: Biophysics Reports Editorial Office
      Keywords: Tension, Optical tweezers, Molecular force

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          Abstract

          Optical tweezers have elucidated numerous biological processes, particularly by enabling the precise manipulation and measurement of tension. One question concerns the biological relevance of these experiments and the generalizability of these experiments to wider biological systems. Here, we categorize the applicability of the information garnered from optical tweezers in two distinct categories: the direct relevance of tension in biological systems, and what experiments under tension can tell us about biological systems, while these systems do not reach the same tension as the experiment, still, these artificial experimental systems reveal insights into the operations of biological machines and life processes.

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          Folding-unfolding transitions in single titin molecules characterized with laser tweezers.

          M S Kellermayer, S B Smith, H L Granzier … (1997)
          Titin, a giant filamentous polypeptide, is believed to play a fundamental role in maintaining sarcomeric structural integrity and developing what is known as passive force in muscle. Measurements of the force required to stretch a single molecule revealed that titin behaves as a highly nonlinear entropic spring. The molecule unfolds in a high-force transition beginning at 20 to 30 piconewtons and refolds in a low-force transition at approximately 2.5 piconewtons. A fraction of the molecule (5 to 40 percent) remains permanently unfolded, behaving as a wormlike chain with a persistence length (a measure of the chain's bending rigidity) of 20 angstroms. Force hysteresis arises from a difference between the unfolding and refolding kinetics of the molecule relative to the stretch and release rates in the experiments, respectively. Scaling the molecular data up to sarcomeric dimensions reproduced many features of the passive force versus extension curve of muscle fibers.
          Article 0 comments Cited 213 times – based on 0 reviews     Review now
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            Tension directly stabilizes reconstituted kinetochore-microtubule attachments.

            James Powers, Hugo Arellano, Jeffrey Ranish … (2010)
            Kinetochores are macromolecular machines that couple chromosomes to dynamic microtubule tips during cell division, thereby generating force to segregate the chromosomes. Accurate segregation depends on selective stabilization of correct 'bi-oriented' kinetochore-microtubule attachments, which come under tension as the result of opposing forces exerted by microtubules. Tension is thought to stabilize these bi-oriented attachments indirectly, by suppressing the destabilizing activity of a kinase, Aurora B. However, a complete mechanistic understanding of the role of tension requires reconstitution of kinetochore-microtubule attachments for biochemical and biophysical analyses in vitro. Here we show that native kinetochore particles retaining the majority of kinetochore proteins can be purified from budding yeast and used to reconstitute dynamic microtubule attachments. Individual kinetochore particles maintain load-bearing associations with assembling and disassembling ends of single microtubules for >30 min, providing a close match to the persistent coupling seen in vivo between budding yeast kinetochores and single microtubules. Moreover, tension increases the lifetimes of the reconstituted attachments directly, through a catch bond-like mechanism that does not require Aurora B. On the basis of these findings, we propose that tension selectively stabilizes proper kinetochore-microtubule attachments in vivo through a combination of direct mechanical stabilization and tension-dependent phosphoregulation.
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              Force and velocity measured for single molecules of RNA polymerase.

              M Wang, M. J. Schnitzer, H. Yin … (1998)
              RNA polymerase (RNAP) moves along DNA while carrying out transcription, acting as a molecular motor. Transcriptional velocities for single molecules of Escherichia coli RNAP were measured as progressively larger forces were applied by a feedback-controlled optical trap. The shapes of RNAP force-velocity curves are distinct from those of the motor enzymes myosin or kinesin, and indicate that biochemical steps limiting transcription rates at low loads do not generate movement. Modeling the data suggests that high loads may halt RNAP by promoting a structural change which moves all or part of the enzyme backwards through a comparatively large distance, corresponding to 5 to 10 base pairs. This contrasts with previous models that assumed force acts directly upon a single-base translocation step.
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                Author and article information

                Contributors
                Matthew T. J. Halma
                Journal
                Journal ID (nlm-ta): Biophys Rep
                Journal ID (iso-abbrev): Biophys Rep
                Journal ID (publisher-id): BR
                Title: Biophysics Reports
                Publisher: Biophysics Reports Editorial Office (Beijing China )
                ISSN (Print): 2364-3439
                ISSN (Electronic): 2364-3420
                Publication date (Print): 29 February 2024
                Volume: 10
                Issue: 1
                Pages: 48-56
                Affiliations
                [1 ] Department of Physics and Astronomy and LaserLab, Vrije Universiteit Amsterdam, De Boelelaan 1081, 1081 HV, Amsterdam, the Netherlands
                [2 ] LUMICKS B. V., 1081 HV, Amsterdam, the Netherlands
                Author notes
                m.t.j.halma@ 123456vu.nl (M. T. J. Halma)

                #Matthew T.J. Halma and Longfu Xu contributed equally to this work.

                Article
                Publisher ID: br-10-1-48
                DOI: 10.52601/bpr.2023.230019
                PMC ID: 11079598
                SO-VID: 8fde1449-e77a-4d52-8ed3-f870c2ef0cab
                Copyright © © The Author(s) 2024
                License:

                This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

                History
                Date received : 11 October 2023
                Date accepted : 6 December 2023
                Categories
                Subject: Commentary

                Keywords: tension,optical tweezers,molecular force
                Data availability:
                Keywords: tension, optical tweezers, molecular force

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