Titlebar

Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar

 

Heavy Meromyosin Molecules Extending More Than 50 nm above Adsorbing Electronegative Surfaces

Title data

Persson, Malin ; Albet-Torres, Nuria ; Ionov, Leonid ; Sundberg, Mark ; Höök, Fredrik ; Diez, Stefan ; Månsson, Alf ; Balaz, Martina:
Heavy Meromyosin Molecules Extending More Than 50 nm above Adsorbing Electronegative Surfaces.
In: Langmuir. Vol. 26 (15 June 2010) Issue 12 . - pp. 9927-9936.
ISSN 1520-5827
DOI: https://doi.org/10.1021/la100395a

Abstract in another language

In the in vitro motility assay, actin filaments are propelled by surface-adsorbed myosin motors, or rather, myosin motor fragments such as heavy meromyosin (HMM). Recently, efforts have been made to develop actomyosin powered nanodevices on the basis of this assay but such developments are hampered by limited understanding of the HMM adsorption geometry. Therefore, we here investigate the HMM adsorption geometries on trimethylchlorosilane- [TMCS-] derivatized hydrophobic surfaces and on hydrophilic negatively charged surfaces (SiO2). The TMCS surface is of great relevance in fundamental studies of actomyosin and both surface substrates are important for the development of motor powered nanodevices. Whereas both the TMCS and SiO2 surfaces were nearly saturated with HMM (incubation at 120 μg mL−1) there was little actin binding on SiO2 in the absence of ATP and no filament sliding in the presence of ATP. This contrasts with excellent actin-binding and motility on TMCS. Quartz crystal microbalance with dissipation (QCM-D) studies demonstrate a HMM layer with substantial protein mass up to 40 nm above the TMCS surface, considerably more than observed for myosin subfragment 1 (S1; 6 nm). Together with the excellent actin transportation on TMCS, this strongly suggests that HMM adsorbs to TMCS mainly via its most C-terminal tail part. Consistent with this idea, fluorescence interference contrast (FLIC) microscopy showed that actin filaments are held by HMM 38 ± 2 nm above the TMCS-surface with the catalytic site, on averge, 20−30 nm above the surface. Viewed in a context with FLIC, QCM-D and TIRF results, the lack of actin motility and the limited actin binding on SiO2 shows that HMM adsorbs largely via the actin-binding region on this surface with the C-terminal coiled-coil tails extending >50 nm into solution. The results and new insights from this study are of value, not only for the development of motor powered nanodevices but also for the interpretation of fundamental biophysical studies of actomyosin function and for the understanding of surface−protein interactions in general.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Engineering Science > Professur Biofabrikation > Professur Biofabrikation - Univ.-Prof. Dr. Leonid Ionov
Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Professur Biofabrikation
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 22 Jun 2017 13:19
Last Modified: 22 Jun 2017 13:19
URI: https://eref.uni-bayreuth.de/id/eprint/37722