Molecular engineering of a backwards-moving myosin motor

Georgios Tsiavaliaris, Setsuko Fujita-Becker and Dietmar J. Manstein ()
Additional contact information
Georgios Tsiavaliaris: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover
Setsuko Fujita-Becker: Abteilung Biophysik, Max-Planck-Institut für Medizinische Forschung
Dietmar J. Manstein: Institut für Biophysikalische Chemie, Medizinische Hochschule Hannover

Nature, 2004, vol. 427, issue 6974, 558-561

Abstract: Abstract All members of the diverse myosin superfamily have a highly conserved globular motor domain that contains the actin- and nucleotide-binding sites and produces force and movement1,2. The light-chain-binding domain connects the motor domain to a variety of functionally specialized tail domains and amplifies small structural changes in the motor domain through rotation of a lever arm3,4. Myosins move on polarized actin filaments either forwards to the barbed (+ ) or backwards to the pointed (- ) end5,6. Here, we describe the engineering of an artificial backwards-moving myosin from three pre-existing molecular building blocks. These blocks are: a forward-moving class I myosin motor domain, a directional inverter formed by a four-helix bundle segment of human guanylate-binding protein-1 and an artificial lever arm formed by two α-actinin repeats. Our results prove that reverse-direction movement of myosins can be achieved simply by rotating the direction of the lever arm 180°.

Date: 2004
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature02303 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:427:y:2004:i:6974:d:10.1038_nature02303

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature02303

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().