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com
ScienceDirect
The unique enzymatic and mechanistic properties
of plant myosins
Arnon Henn1 and Einat Sadot2
Myosins are molecular motors that move along actin-filament
tracks. Plants express two main classes of myosins, myosin VIII
and myosin XI. Along with their relatively conserved sequence
and functions, plant myosins have acquired some unique
features. Myosin VIII has the enzymatic characteristics of a
tension sensor and/or a tension generator, similar to functions
found in other eukaryotes. Interestingly, class XI plant myosins
have gained a novel function that consists of propelling the
exceptionally rapid cytoplasmic streaming. This specific class
includes the fastest known translocating molecular motors,
which can reach an extremely high velocity of about
60 mm s1. However, the enzymatic properties and
mechanistic basis for these remarkable manifestations are not
yet fully understood. Here we review recent progress in
understanding the uniqueness of plant myosins, while
emphasizing the unanswered questions.
Addresses
1
Faculty of Biology, Technion-Israel Institute of Technology, Haifa
3200003, Israel
2
The Institute of Plant Sciences, Volcani Center, PO Box 6, Bet-Dagan
5025000, Israel
Corresponding authors: Henn, Arnon (arnon.henn@technion.ac.il) and
Sadot, Einat (vhesadot@agri.gov.il)
Current Opinion in Plant Biology 2014, 22:65–70
This review comes from a themed issue on Cell biology
Edited by Shaul Yalovsky and Viktor Žárský
For a complete overview see the Issue and the Editorial
Available online 2nd October 2014
http://dx.doi.org/10.1016/j.pbi.2014.09.006
1369-5266/# 2014 Elsevier Ltd. All rights reserved.
Introduction
Live-cell imaging of plant cells reveals strikingly rapid
movement of organelles and vesicles, rearrangement of
the endoplasmic reticulum (ER) and constant remodeling
of the tonoplast. Under certain conditions slower move-
ment of the chloroplasts and nucleus can also be observed.
This intracellular dynamic is believed to enable the immo-
tile plant to respond quickly to abiotic and biotic stresses.
The machinery underlying these vigorous movements
involves actin-based molecular motors, the myosins and
actin microfilaments that together drive the formation of
streaming patterns in plant cells. Myosins utilize ATP to
perform mechanical work such as muscle contraction and
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the translocation of cargo along actin filaments in eukaryotic
cells [1]. Across all eukaryotes there are 35 known classes of
myosins [2]. In plants there are two main classes, VIII, XI
[3], which are widely distributed in higher and lower plants.
Plant myosins are involved in various organelles’ motility
[4,5,6–14], ER remodeling [15–18] and cytoplasmic
streaming [19,20,21,22]. They have been found in
the plasmodesmata [23–25,26] and can be involved in
targeted RNA transport [27], viral spread from cell to cell
[28–31] and in a plant’s size and shape determination
[6,22,32]. All known myosins share a highly conserved
amino-terminal motor domain followed by a neck (also
referred to as the ‘lever arm’) and the tail regions. The
neck region, which contains conserved IQ repeats (as many
as one to six in tandem), serves as the light chains binding
domains and the tail region which displays diverse inter-
acting domains such as cargo and membrane binding motifs
[1]. The myosin actin-dependent ATPase cycle includes at
least six nucleotide-linked, biochemical intermediates
(Figure 1a). The cycling of myosin on actin is driven by
ATP binding, hydrolysis and product release, and can be
described as follows (Figure 1a from left to right): ATP
binding to actomyosin causes myosin head to dissociate
from actin. Detached myosin hydrolyzes ATP to ADP and
Pi, which drives the repriming of the lever arm to the ‘pre-
power stroke’ state. This post hydrolysis state can rebind
actin with a higher affinity than before the hydrolysis of
ATP. Upon the rebinding of myosin-ADP-Pi state to actin
conformational changes within the myosin motor domain
are coupled to the release of Pi and the lever arm rotation
relative to the actin-bound myosin head. This lever arm
rotation transition is the force-generating step, or the
‘power-stroke’, of the myosin ATPase cycle, which is next
followed by ADP release, and the formation of the myosin-
actin nucleotide free state. Thereafter, the catalytic cycle
begins again with ATP binding. Specific nucleotide states
dictate the affinity of the myosin motor domain towards
actin. The strength of the myosin nucleotide binding states
towards actin follows from strong to weak binding affinities
as such: actomyosin > actomyosin-ADP > actomyosin-
ADP-Pi > actomyosin-ATP. Although this ATPase cycle
kinetic pathway is highly conserved among all myosins
studied to date, the enzymatic properties of the catalytic
motor domain display very large deviations in their kinetic
and thermodynamic properties, that is, each myosin isoform
displays different rate and equilibrium constants for the
biochemical transitions described in Figure 1a [33,34].
These different rate and equilibrium constants give raise
to different ATPase cycling-times, affinities toward actin
and motility rates among myosins. They are the hallmarks
Current Opinion in Plant Biology 2014, 22:65–70
66 Cell biology

Figure 1

(a) Myosin XIChara: Myosin V, VIII:

Very fast ADP release Rate limiting Step
during ATPase
cycling

“Strongly Bound” “Weakly Bound” “Strongly Bound”

K’H K’Pi
AM + ATP AM ATP AM ADP Pi AM ADP AM + ADP

KA KAPi KAD KA
KT KH KPi KD
M + ATP M ATP M ADP Pi M ADP M + ADP

“Dissociated States” “Thermodynamic Coupling box”

(b) Low TC for Myosin V, VIII

High TC for Myosin XIChara.
Second strongly bound
actomyosin-ADP state

“Strongly Bound”

K’D1 K’D2
AM ADP AM ADP’ AM + ADP

Slow isomerization

Current Opinion in Plant Biology

The actomyosin ATPase cycle. (a) Schematic representation of myosin’s conserved chemomechanical energy transduction pathway is shown. The
reaction pathway in the black frame is the predominant pathway for the myosin ATPase cycle as described in the text. Key features in plant myosins
VIII and XIChara in relation to the ATPase reaction scheme are shown. The dashed blue frame contains the key parameters for determining
thermodynamic coupling (TC) between actin and ADP affinities toward myosin. Black and blue callouts mark unique features among measured
parameters of plant myosins. Blue ovals highlight extremely rapid rate constants for Chara myosin XI. Red ovals mark rate and equilibrium constants
that have not been measured for any plant myosin. (b) Expansion of the minimal kinetic scheme showing the transition from actomyosin-ADP to
actomyosin with additional intermediate ADP state namely actomyosin-ADP0 indicative of tension-sensor myosins.

of the diverse enzymatic behavior among the myosin family
classes and isoforms. In turns, these unique features enables
each myosin isoform to be enzymatically adapted to its
cellular functions. Here we describe the findings related to
the motor properties of the two main classes of plant
myosins and discuss their enzymatic adaptation to the
relevant unique cellular functions in plants.
Class VIII myosins
The first plant myosin to be cloned and sequenced was
Arabidopsis thaliana myosin 1 (ATM1). Phylogenetic
analysis based on its motor domain placed ATM1 in a
new myosin class VIII [35]. Specific antibodies against its
tail domain revealed its subcellular localization in the
plasmodesmata and newly formed cell plates in the roots
of maize and cress (Lepidium sativum) [36]. Subsequent
green fluorescent protein (GFP) fusions confirmed these
observations [25,26,37], and also suggested its localiz-
ation in ER junctions [25]. Analysis of the knockout plant
of all five myosin VIII transcripts of P. patens revealed
that this class has a role in development and hormone
homeostasis [32]. Recent detailed transient kinetic and
thermodynamic studies of myosin VIII have revealed its
enzymatic properties [26]. It was found that ADP
release (at physiological levels of Mg2+) [26] is the
rate-limiting step (the slowest transition within one com-
plete ATPaes cycle, Figure 1a) in myosin VIII’s ATPase
cycle, which contributes to the long-lived and strongly-
bound actomyosin-ADP state during the ATPase cycle
and to high duty ratio (DR — see below). The cycling
time is defined as a single complete cycle of ATP binding,
hydrolysis and product release (Figure 1a). Myosin VIII
displays a relatively slow to moderate ATPase cycle, with
a slow motility rate that is highly regulated by Mg2+
[26]. The latter characterize local tension-bearing myo-
sins rather than fast moving transporters [33,38]. In
addition, the two states, with fast and slow dissociation
rates (Figure 1b), observed in myosin VIII [26] suggest
that additional work can be achieved with the slower step
of ADP dissociation [38]. This is a unique feature that is
found in several tension-sensor myosins [33]. Further-
more, myosin VIII displays a very weak thermodynamic

Current Opinion in Plant Biology 2014, 22:65–70 www.sciencedirect.com


coupling (TC) ratio of 2.3 [26]. TC is a measure of how
the affinity of myosin to actin is affected by its binding to
ADP, in comparison to how its binding to ADP is affected
by actin. This simply reflects the degree of communi-
cation between the nucleotide and actin binding sites,
and is derived from the free energy detailed balance of
the ADP states. Detailed balance requires that in the
absence of external energy input or consumption the
product of the four equilibrium constants equal unity
and, therefore, K 0D =K D ¼ K A =K AD (Figure 1a). Tension-
sensor myosins have been shown to display very weak TC
or a low ratio close to unity between the equilibrium
constants [33,38]. A weak TC permits strong binding to
actin in the presence of ADP, and hence to bear tension in
the strongly bound ADP states. Lastly, the kinetic adap-
tation of plant myosin VIII for its function also stems from
its measured high DR of 0.9 [26]. The DR is defined as
the fraction of time that myosin spends strongly bound to
actin during the complete ATPase cycle. Thus, the
detailed enzymological studies of myosin VIII strongly
suggest that it is enzymatically adapted to maintaining
tension, such as that required for ER tethering to the
plasma membrane for proper plasmodesmatal function
[39]. However, the latter assumption requires in-vivo
validations.
Class XI myosins
Class XI myosins from Chara corallina are the fastest
actin-based motors characterized to date, even faster than
myosin XI members in higher plants. Class XI myosins
show sequence and structural similarities to vertebrates’
transporter class V myosins [40]. Both contain a long lever
arm composed of six IQ motifs, indicative of a large step
size, and a coiled-coil motif, which favors a double-
headed (dimer) myosins’ oligomeric state [41]. Despite
these similarities to myosin class V, the velocity measure-
ments by in vitro motility assay for plant myosins have
demonstrated remarkably higher rates. For purified C.
corallina myosin XI, the measured velocities range from
20 mm s1 up to 60 mm s1 [42–44], and for myosin XI
from Nicotiana tabacum and Arabidopsis this is about
7 mm s1. These measurements are up to 150-folds and
20-folds respectively, faster than myosin V [45]. Purified
myosin XI from N. tabacum was found to have a step size
of 35 nm [46]. This step size was similar to that
measured for myosin V, which has an identical lever
arm length of six IQ motifs [45]. The step size measured
for the faster Chara myosin XI was 19 nm [44]. The
extraordinarily high velocity of myosin XI does not result
from an unusually large step size. Calculations combining
velocity with step size suggested that the ATPase cycling
time for the slower measured velocity (myosin XI from N.
tabacum and Arabidopsis) should be 200 ATP s1 h1
(s1 h1 is define as moles of ATP hydrolyzed per second
per head, that is, a head is a single motor domain, 200 is
calculated from the measured values of 7 mm s1 per
35 nm stepsize) and 1052 ATP s1 h1 (20 mm s1 per
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Plant myosins Henn and Sadot 67
19 nm) for the faster measured velocity (Chara myosin
XI). Interestingly, the fastest measured actin-activated
ATPase rate for N. tabacum myosin XI was
76 ATP s1 h1 [46], and for Chara myosin XI,
670  20 ATP s1 h1 [47]. Detailed enzymology for N.
tabacum myosin XI is still lacking, but it will be interesting
to see how it supports not only rapid velocity but also a
sufficiently high DR (0.8 [46]) for its processive move-
ment (the ability to take multiple steps along actin before
dissociating). Detailed transient kinetic measurements
were performed on the motor domain of Chara myosin
to reveal its ATPase reaction mechanism; some interest-
ing features were found that might support the rapid
ATPase cycling time [48]. Chara myosin, that was shown
to posses a 19 nm step size exhibits an extremely rapid
ADP-dissociation rate (>2800 s1), fast ATP-binding rate
(36 mM1 s1) and ATP-induced dissociation from actin
(2200 s1), as well as very rapid ATP hydrolysis
(>530 s1). However, it dwells in the strongly bound
state for less than 0.82 ms, which is a very short lifespan
with respect to its full ATPase cycling time of 2.5 ms
calculated from the ATPase rate (kcat of 390 s1). Further-
more, its low DR of <0.3 may not support high proces-
sivity or long run length, as seen for N. tabacum [33,34].
For Chara myosin XI, the super-fast transitions could
support rapid ATP turnover within the range of the
suggested actin-gliding velocity. A structural molecular
basis for the extremely short cycling time was tested
experimentally by mutating the properties of loops
2 and 3 in the motor domain of Chara myosin XI which
are known to be part of the actin-binding site. Yamamoto
and co-workers [47] identified a net charge of zero for loop
2, with no lysine cluster, unlike in myosin V. In addition,
it was found that loop 3 had a high positive charge and was
the largest in size of all known myosins [47]. Loop 2 is also
important for the myosin-ADP-Pi state binding to actin
[47]. In this study the authors provide new insights
regarding these two loops. Firstly, the interaction of Chara
myosin XI with actin is mediated mainly by loop 3 and
secondly, it does not hinder rapid release of ADP. In
contrast, they found that lengthening loop 2 slows down
ADP release, which had not been shown before. There-
fore, the authors suggest that it is this unique combination
of zero net charge of a short sequence in loop 2 with a very
long loop 3 which facilitates the high ATPase rate necess-
ary to support the very high velocity [47]. However, more
work is needed to elucidate additional unique features of
the extremely fast ATPase cycle. Based on the above
data, the myosin XI ATPase cycling time is <1 ms while
that of myosin V is on the order of 65 ms [49]. This time
scale for Chara myosin requires that most kinetic tran-
sitions and binding events in the cycle (Figure 1a) be near
diffusion-limited reaction rate constants. In other words,
some Chara class XI myosins exhibit near kinetic perfec-
tion, which is often assessed by the specificity constant,
kcat/Km in the order of 108–109 M1 s1 [50]. For the
fastest Chara, the calculated specificity constant is on
Current Opinion in Plant Biology 2014, 22:65–70
68 Cell biology
the order of 50  106 M1 s1 [44,50], which is con-
siderably slower than for the lower limit for such diffu-
sion-limited reaction rate constants. Thus, this alone
cannot account for the high efficiency and fast ATPase
cycling of Chara myosin. Furthermore, structural confor-
mational changes, such as opening and closing of the
nucleotide-binding and actin-binding clefts, take on the
order of milliseconds and are therefore too slow to allow
such rapid ATPase cycling [51]. More structural studies
and dynamic investigation of the actin-binding and
nucleotide-binding clefts may provide further structural
basis for the observed rapid transition and binding of
nucleotides and actin to Chara myosin from class XI.
The mechanism by which myosins propel
cytoplasmic streaming
In comparison to other myosin classes the biomechanical
properties of plant myosins are not their only unique
feature, since the way they propel the movement of large
organelles might also be different. It is believed that the
motion of organelles associated with myosin motor
proteins along actin cables propels the viscous cyto-
plasmic fluid [21,52]. The speed of cytoplasmic stream-
ing in Arabidopsis, N. benthamiana, and in Chara,
resembles the speed of myosin XI from these plants in
in vitro motility assays [53]. However, it is still not clear
which organelles are directly associated with myosins to
propel the cytoplasmic streaming. While some studies
have found that GFP fusions to fragments from various
myosin XI tail domains colocalize to known organelles
[54–56], other studies have shown no such colocalization
[5,11,13,14]. An active full-length myosin XIK from
Arabidopsis fused to GFP was found to interact solely
with specific unknown transport vesicles via specific
myosin-binding proteins, myoB1/2 [5]. Moreover, the
movement of the transport vesicles was fast and constant
along the actin fibers, whereas that of known organelles
was characterized by stochastic changes in speed and
direction [11,12,14]. Thus, cytoplasmic streaming was
suggested to be created by the special transport vesicles
associated with myosin XIK, while the other organelles
merely drifted in the hydrodynamic flow or, alternatively,
were transiently associated with the transport vesicles
[5]. Since load is known to affect myosin functioning
[33], it would be intriguing to determine whether the
specific transport vesicles are adjusted to facilitate the
super speed velocity of class XI plant myosins, thus
constituting another component of the fast and efficient
mechanism.
Conclusions
Myosins are divided into two groups: conventional, in-
cluding class II myosins and unconventional, which in-
clude plant myosins, among many others. However, plant
myosins seem to be highly unconventional within the
group of unconventional myosins. Some of the evolved
biological, biochemical and biophysical optimizations
Current Opinion in Plant Biology 2014, 22:65–70
that underlie the manifestations of plant myosins remain
to be determined.
Acknowledgements
The authors apologize to all colleagues whose important contributions could
not be highlighted or discussed herein due to space limitations. We thank
our group members for their critical reading of the manuscript and
invaluable comments. ES acknowledges a grant from the Israeli Science
Foundation (ISF) 401/09. AH acknowledges the Marie Curie Career
Integration Grant 1403705/11.
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