A Longitudinal-Bending Hybrid Linear Ultrasonic Motor and Its Driving Characteristic

As a new type of driver, linear ultrasonic motor (LUSM) is widely used in the high-tech field because of its low speed, high thrust, low noise, and no electromagnetic interference. However, as an actuator used in microdevices, most of the existing LUSMs are large in size and not compact in structure. In order to overcome these limitations, a new structure of linear ultrasonic motor’s stator is developed in this paper. The stator is similar to a tuning fork structure, which is divided into three parts: two driving feet, two driving legs, and the driving body. By using the first-order longitudinal vibration mode of the whole stator and the unique partial second-order bending vibration mode of the driving legs to achieve vibration mode degeneracy, a mode hybrid linear ultrasonic motor that is easy to miniaturize is proposed. Its working principle is analyzed. The dynamic analysis of the stator is carried out by using finite element software. The structure dimension of the stator and the driving frequency under the working mode are determined. At the same time, the feasibility of driving feet synthesizing elliptical motion is verified theoretically and experimentally. In addition, the LUSM test setup is built. The effects of driving frequency and Vpp on stator stall force and average velocity are studied. The results show that the maximum stall force can reach 99 mN, and the average velocity of the motor is 88.67 mm/s with Vpp = 320 V and driving frequency 80.2 kHz. The proposed LUSM is appropriate for use in occasions with quick return characteristics, like the controlling valve or nozzle of the printer. The research results provide guidance for the stator design of the linear ultrasonic motor.

Force and Stepwise Movements of Gliding Motility in Human Pathogenic Bacterium Mycoplasma pneumoniae

Mycoplasma pneumoniae, a human pathogenic bacterium, binds to sialylated oligosaccharides and glides on host cell surfaces via a unique mechanism. Gliding motility is essential for initiating the infectious process. In the present study, we measured the stall force of an M. pneumoniae cell carrying a bead that was manipulated using optical tweezers on two strains. The stall forces of M129 and FH strains were averaged to be 23.7 and 19.7 pN, respectively, much weaker than those of other bacterial surface motilities. The binding activity and gliding speed of the M129 strain on sialylated oligosaccharides were eight and two times higher than those of the FH strain, respectively, showing that binding activity is not linked to gliding force. Gliding speed decreased when cell binding was reduced by addition of free sialylated oligosaccharides, indicating the existence of a drag force during gliding. We detected stepwise movements, likely caused by a single leg under 0.2-0.3 mM free sialylated oligosaccharides. A step size of 14-19 nm showed that 25-35 propulsion steps per second are required to achieve the usual gliding speed. The step size was reduced to less than half with the load applied using optical tweezers, showing that a 2.5 pN force from a cell is exerted on a leg. The work performed in this step was 16-30% of the free energy of the hydrolysis of ATP molecules, suggesting that this step is linked to the elementary process of M. pneumoniae gliding. We discuss a model to explain the gliding mechanism, based on the information currently available.

Autoregulation and Dual Stepping Mode of MYA2, an Arabidopsis Myosin XI Responsible for Cytoplasmic Streaming

Arabidopsis thaliana has 13 genes belonging to the myosin XI family. Myosin XI-2 (MYA2) plays a major role in the generation of cytoplasmic streaming in cells. In this study, we investigated the molecular properties of MYA2 expressed by the baculovirus transfer system. Actin-activated ATPase activity and in vitro motility assays revealed that activity of MYA2 was regulated by the globular tail domain (GTD), When the GTD is not bound to the cargo, the GTD inhibits ADP dissociation from the motor domain. Optical nanometry of single MYA2 molecules, combining TIRF microscopy and the FIONA method, revealed that the MYA2 processively moved on actin with three different step sizes: −28 nm, 29 nm, and 60 nm, at low ATP concentrations. This result indicates that MYA2 uses two different stepping modes, hand-over-hand and inchworm-like. Force measurement using optical trapping showed the stall force of MYA2 was 0.85 pN, which was less than half that of myosin V (2 − 3 pN). These results indicated that MYA2 is more flexible than the myosin V responsible for vesicle transport in animal cells. Such flexibility may enable multiple myosin XIs to transport organelles quickly and smoothly, for the generation of cytoplasmic streaming in plant cells.

Force and step size of gliding motility in human pathogenic bacterium Mycoplasma pneumoniae

Mycoplasma pneumoniae, a human pathogenic bacterium, binds to sialylated oligosaccharides and glides on host cell surfaces via a unique mechanism. Gliding motility is essential for initiating the infectious process. In the present study, we measured the stall force of an M. pneumoniae cell carrying a bead that was manipulated using optical tweezers on two strains. The stall forces of M129 and FH strains were averaged to be 23.7 and 19.7 pN, respectively, much weaker than those of other bacterial surface motilities. The binding activity and gliding speed on sialylated oligosaccharides of the M129 strain were eight and two times higher than those of the FH strain, respectively, showing that binding activity is not linked to gliding force. Gliding speed decreased when cell binding was reduced by addition of free sialylated oligosaccharides, indicating the existence of a drag force during gliding. We detected stepwise movements under 0.2‒0.3 mM free sialylated oligosaccharides. A step size of 14‒19 nm showed that 25‒35 propulsion steps per second are required to achieve the usual gliding speed. The step size was reduced to less than half with the load applied using optical tweezers, showing that a 2.5 pN force from a cell is exerted on a leg. The work performed in this step was 16‒30% of the free energy of the hydrolysis of ATP molecules, suggesting that this step is linked to the elementary process of M. pneumoniae gliding.

The Study on Simulation of Resistance in Stall Motor

The stall phenomenon which happens in loaded motor is unqualification in application. Meanwhile it may measure the maximum property of motor in manufacture. So the phenomenon is analyzed to find a simulation of electrical state to predict the maximum currency and torque which is a necessary method to be proceeded up to now before design. We find that the simulation fits well to the reference. The conditions of t=60s,U=22V result in the biggest stall force according to rotation to change time and voltage. Then it is t=90s,U=17V; t=30s,U=27V and t=120s,U=12V in turns. As for torque it is t=30s,U=27V; t=60s,U=22V;t=90s,U=17V and t=120s,U=12V in truns.

Force production of human cytoplasmic dynein is limited by its processivity

Cytoplasmic dynein is a highly complex motor protein that generates forces toward the minus end of microtubules. Using optical tweezers, we demonstrate that the low processivity (ability to take multiple steps before dissociating) of human dynein limits its force generation due to premature microtubule dissociation. Using a high trap stiffness whereby the motor achieves greater force per step, we reveal that the motor’s true maximal force (“stall force”) is ~2 pN. Furthermore, an average force versus trap stiffness plot yields a hyperbolic curve that plateaus at the stall force. We derive an analytical equation that accurately describes this curve, predicting both stall force and zero-load processivity. This theoretical model describes the behavior of a kinesin motor under low-processivity conditions. Our work clarifies the true stall force and processivity of human dynein and provides a new paradigm for understanding and analyzing molecular motor force generation for weakly processive motors.

FliI6-FliJ molecular motor assists with unfolding in the type III secretion export apparatus

The role of rotational molecular motors of the ATP synthase class is integral to the metabolism of cells. Yet the function of FliI6-FliJ complex - a homolog of the F1 ATPase motor - within the flagellar export apparatus remains unclear. We use a simple two-state model adapted from studies of linear molecular motors to identify key features of this motor. The two states are the ‘locked’ ground state where the FliJ coiled coil filament experiences fluctuations in an asymmetric torsional potential, and a ‘free’ excited state in which FliJ undergoes rotational diffusion. Michaelis-Menten kinetics was used to treat transitions between these two states, and obtain the average angular velocity of the FliJ filament within the FliI6 stator: ωmax ≈ 9.0 rps. The motor was then studied under external counter torque conditions in order to ascertain its maximal power output: Pmax ≈ 42 kBT/s, and the stall torque: Gstall ≈ 3 kBT/rad. Two modes of action within the flagellar export apparatus are proposed, in which the motor performs useful work either by continuously ‘grinding’ through the resistive environment, or by exerting equal and opposite stall force on it. In both cases, the resistance is provided by flagellin subunits entering the flagellar export channel prior to their unfolding. We therefore propose that the function of the FliI6-FliJ complex is to lower the energy barrier and therefore assist in unfolding of the flagellar proteins before feeding them into the transport channel.

The kinesin-8 Kip3 depolymerizes microtubules with a collective force-dependent mechanism

ABSTRACTMicrotubules are highly dynamic filaments with dramatic structural rearrangements and length changes during the cell cycle. An accurate control of the microtubule length is essential for many cellular processes in particular, during cell division. Motor proteins from the kinesin-8 family depolymerize microtubules by interacting with their ends in a collective and length-dependent manner. However, it is still unclear how kinesin-8 depolymerizes microtubules. Here, we tracked the microtubule end-binding activity of yeast kinesin-8, Kip3, under varying loads and nucleotide conditions using high-precision optical tweezers. We found that single Kip3 motors spent up to 200 s at the microtubule end and were not stationary there but took several 8-nm forward and backward steps that were suppressed by loads. Interestingly, increased loads, similar to increased motor concentrations, also exponentially decreased the motors’ residence time at the microtubule end. On the microtubule lattice, loads also exponentially decreased the run length and time. However, for the same load, lattice run times were significantly longer compared to end residence times suggesting the presence of a distinct force-dependent detachment mechanism at the microtubule end. The force dependence of the end residence time enabled us to estimate what force must act on a single motor to achieve the microtubule depolymerization speed of a motor ensemble. This force is higher than the stall force of a single Kip3 motor, supporting a collective force-dependent depolymerization mechanism that unifies the so-called “bump-off” and “switching” models. Understanding the mechanics of kinesin-8’s microtubule end activity will provide important insights into cell division with implications for cancer research.STATEMENT OF SIGNIFICANCEKinesin-8 motors are important for microtubule length regulation and are over-expressed in different types of cancer. Yet, on the molecular level, it is unclear how these motors depolymerize microtubules. Using high-precision optical tweezers, we measured how single yeast kinesin-8 motors, Kip3, interacted with the microtubule end. Interestingly, we found that single Kip3 motors were still motile at the microtubule end. The force dependence of how long single motors were associated with the microtubule end enabled us to estimate what force motors must exert onto each other to achieve the collective microtubule depolymerization speed of many motors. Our data support a collective force-dependent depolymerization mechanism. A better understanding of Kip3’s microtubule end activity has implications for cell division and associated diseases.

An Eight-Zonal Piezoelectric Tube-Type Threaded Ultrasonic Motor Based on Second-Order Bending Mode

In order to reduce the driving voltage and gain better output characteristics of piezoelectric actuators, an eight-zonal piezoelectric tube-type threaded ultrasonic motor based on two second-order bending modes was analyzed using the method of finite element analysis (FEA), and a prototype was fabricated and experimentally studied in this research. This piezoelectric motor was designed to be excited by four electrical sources applied simultaneously to four groups of electrodes on the customized lead zirconate titanate (PZT) tubular stator (inside diameter 5.35 mm, outside diameter 6.35 mm, length 30 mm), with ±90° phase shifts between adjacent electrodes. Experimental results show that the threaded motor could output a stall force (stall force means the output pull or thrust force when the linear speed is set to be zero) of about 5.0 N and a linear velocity of 4.9 mm/s with no load at the driving voltage of 40 Vpp (Vpp means the peak-to-peak value of the voltage volts). This piezoelectric motor with a compact structure and screw drive mechanism shows relatively fine velocity controllability and has huge superiority in micro-positioning systems.