Strikingly fast microtubule sliding in bundles formed by <i>Chlamydomonas</i> axonemal dynein

Aoyama, Susumu; Kamiya, Ritsu

doi:10.1002/cm.20450

Cited by 17 publications

(18 citation statements)

References 34 publications

(65 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…S1, B and C) (7). Evidence from a previous study showed that the microtubule sliding is strikingly fast if OADs are aligned in bundles (8). Besides, our reconstitution assay reveals that ordered OAD arrays can be spontaneously formed in the presence of MTD, in line with a previous finding (6).…”

supporting

confidence: 90%

See 1 more Smart Citation

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Rao

Wang

Chai

et al. 2020

Preprint

View full text Add to dashboard Cite

Thousands of outer-arm dyneins (OADs) are arrayed in the axoneme to drive a rhythmic ciliary beat. Using electron microscopy, we determined the structure of OAD array bound to microtubule doublets (MTDs) in near-atomic details and illuminate how OADs coordinate with each other to move one step forward. OAD prefers a specific pattern of MTD protofilaments for its distinct microtubule-binding domains. Upon MTD binding, free OADs are induced to adopt a stable parallel conformation, primed for array formation. Extensive tail-to-head (TTH) interactions between OADs are observed, which need to be broken for ATP turnover by the dynein motor. ATP-hydrolysis in turn relaxes the TTH interfaces to sequentially effectuate free nucleotide cycle of downstream OADs. These findings lead to a model for how conformational changes of OADs produce coordinated actions.

show abstract

supporting

confidence: 90%

“…1a and 1b) (25, 26) . Early evidence showed that the microtubule sliding is strikingly fast if OADs are aligned in bundles (27) . Studies also revealed that the sliding could be ceased by blockage of several adjacent OADs, suggesting OADs are successively activated along an MTD (19) .…”

Section: Resultsmentioning

confidence: 99%

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Rao

Wang

Chai

et al. 2020

Preprint

View full text Add to dashboard Cite

show abstract

“…The velocity was variable (Fig S2B ), with some MTs sliding much faster than those observed in gliding assays. Fast sliding was previously observed with similar dynein-MT complexes but with much higher concentration of dynein, and was interpreted as the effect of cooperation of dyneins aligned with the 24-nm periodicity (Aoyama & Kamiya, 2010).…”

Section: Motile Properties Of the Dynein-mt Complexsupporting

confidence: 66%

Oscillatory movement of a dynein-microtubule complex crosslinked with DNA origami

Hirose

Higuchi

Abdellatef

et al. 2021

Preprint

View full text Add to dashboard Cite

During repetitive bending of cilia and flagella, axonemal dynein molecules move in an oscillatory manner along a microtubule (MT), but how the minus-end-directed motor dynein can oscillate back and forth is unknown. There are various factors that may regulate the dynein activities, e.g., the nexin-dynein regulatory complex, radial spokes, and central apparatus. In order to understand the basic mechanism of the oscillatory movement, we constructed a simple model system composed of MTs, outer-arm dyneins, and DNA origami that crosslinks the MTs. Electron microscopy (EM) showed patches of dynein molecules crossbridging two MTs in two opposite orientations; the oppositely oriented dyneins are expected to produce opposing forces. The optical trapping experiments showed that the dynein-MT-DNA-origami complex actually oscillate back and forth after photolysis of caged ATP. Intriguingly, the complex, when held at one end, showed repetitive bending motions. The results show that a simple system composed of ensembles of oppositely oriented dyneins, MTs, and inter-MT crosslinkers, without any additional regulatory structures, has an intrinsic ability to cause oscillation and repetitive bending motions.

show abstract

“…As reported previously, flagellar outer-arm dynein molecules are aligned on a microtubule in a selforganizing manner with the interval of 24 nm (30,31). Furthermore, the dense cluster of dynein molecules on a microtubule enables the complex to travel a long distance along another microtubule (>10 μm) toward the minus end in the presence of ATP (32,33). For example, ∼40 dynein molecules can be mounted linearly even on 1-μm microtubule fragments and interact with a track microtubule cooperatively.…”

Section: Significancementioning

confidence: 54%

Self-organized optical device driven by motor proteins

Aoyama

Shimoike

Hiratsuka

2013

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Protein molecules produce diverse functions according to their combination and arrangement as is evident in a living cell. Therefore, they have a great potential for application in future devices. However, it is currently very difficult to construct systems in which a large number of different protein molecules work cooperatively. As an approach to this challenge, we arranged protein molecules in artificial microstructures and assembled an optical device inspired by a molecular system of a fish melanophore. We prepared arrays of cell-like microchambers, each of which contained a scaffold of microtubule seeds at the center. By polymerizing tubulin from the fixed microtubule seeds, we obtained radially arranged microtubules in the chambers. We subsequently prepared pigment granules associated with dynein motors and attached them to the radial microtubule arrays, which made a melanophore-like system. When ATP was added to the system, the color patterns of the chamber successfully changed, due to active transportation of pigments. Furthermore, as an application of the system, image formation on the array of the optical units was performed. This study demonstrates that a properly designed microstructure facilitates arrangement and selforganization of molecules and enables assembly of functional molecular systems.bioengineering | microdevice | molecular robotics W ithin a cell, motor proteins work as mechanical components that efficiently convert chemical energy to mechanical energy. Major motor proteins, such as myosin, kinesin, and dynein, travel unidirectionally along specific filamentous protein polymers, actin filaments, or microtubules, using the chemical energy derived from ATP. Although the action of motor proteins itself is rather simple, they are involved in numerous functions in living cells such as cell division, muscle contractions, ciliary beating, and melanophore color changes (1). These diverse and elaborate functions are realized through highly ordered molecular systems that consist of not only the motor proteins but also various types of protein molecules. For example, myosin and actin form alternatively arranged bundles with tens of other proteins to construct aligned sarcomeres, the basic units of the muscle, which produce efficient contractions under strict Ca 2+ regulation (1). Likewise, in the cilium or flagellum, dynein molecules are integrated into the "9 + 2" arrangement of microtubules and generate oscillatory bending (1). Thus, diversity of in vivo functions of motor proteins is achieved by the variety of manners in which motor proteins are organized into specific higher order systems.In the last decade, remarkable progress has been made in the applications of motor proteins in microscale and nanoscale engineering, which has enabled the control of motor protein movements and the transport of artificial objects by motor protein (2-14). These microtransportation systems are expected to be a shuttle for micrototal analysis systems and other simple tools (15)(16)(17). To fully use the potential...

show abstract

Strikingly fast microtubule sliding in bundles formed by Chlamydomonas axonemal dynein

Cited by 17 publications

References 34 publications

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Structures of outer-arm dynein array on microtubule doublet reveal a motor coordination mechanism

Oscillatory movement of a dynein-microtubule complex crosslinked with DNA origami

Self-organized optical device driven by motor proteins

Contact Info

Product

Resources

About