MYOSIN POWERED CELL

MOVEMENTS

TOPICS TO COVER

Why Myosin
Types of Myosin
Structure of Myosin
Activity of Myosin
Actin Myosin Motion

WHY MYOSIN?
Interactions between myosin II and actin
filaments
are
responsible
for
muscle
contraction.
As biologists investigated various types of cell
movements, it became clear that myosin II
mediates only a few types, such as cytokinesis
and muscle contraction.
Other types of cell movements, including
vesicle transport, membrane extension, and
the movement of chromosomes, require either
other myosin isoforms, other motor proteins
such as kinesin or dynein, or actin
polymerization.

CONTRACTION OF MUSCLES
Contraction, the special form of
movement
resulting
from
the
interaction of actin and myosin II, is
most highly evolved in skeletal
muscle cells. However, somewhat
similar contractile events entailing
less organized systems are found in
nonmuscle cells.

Myosins Are a Large Superfamily

of Mechanochemical Motor Proteins

Eight members of the myosin gene family have been identified by genomic
analysis. Three family membersmyosin I, myosin II, and myosin Vare
present in nearly all eukaryotic cells and are the best understood.
Although the specific activities of these myosins differ, they all function as
motor proteins.
myosin II powers muscle contraction, as well as cytokinesis.
Myosins I and V take part in cytoskeletonmembrane interactions, such
as the transport of membrane vesicles.
myosins VI, VII, and XV have functions associated with hearing and hair
cell stereocilia structure.
Plants do not have the same myosins as animal cells.
o Three myosins (VII, XI, and XIII) are exclusively expressed in plants.
o Myosin XI, which may be the fastest myosin of all, is implicated in the
cytoplasmic streaming seen in green algae and higher plants

STRUCTURE OF MYOSIN
Myosin II is assembled into so-called bipolar thick filaments,
containing hundreds of individual myosin II proteins.
They interdigitate with actin filaments to bring about muscle
contraction.
Dissolving myosin in a solution of ATP and high salt yields a
protein of 6 polypeptides
2 heavy chains
4 regulatory light chains
The soluble myosin has ATPase activity.

But which domain of Myosin is responsible for this ATPase

activity?

Figure 34.3. Myosin Dissection. Treatment of muscle myosin with

proteases forms stable fragments, including subfragments S1 and S2 and light
meromyosin. Each S1 fragment includes the head (shown in yellow and pink)
from the heavy chain and one copy of each light chain (shown in blue and
orange).

Figure 34.19. Thick Filament. (A) An electron micrograph of a

reconstituted thick filament reveals the presence of myosin head
domains at each end and a relatively narrow central region.
(B) A schematic view shows how myosin molecules come
together to form the thick filament. [Part A courtesy of Dr. Hugh
Huxley

Myosin Heads Walk Along ActinFilaments

in Discrete Steps

The mechanism of myosin-powered movement was greatly aided by

development of in vitro motility assays.

In one such assay, the sliding-filament assay, the movement of

fluorescence-labeled actin filaments along a bed of myosin molecules is
observed in a fluorescence microscope. Because the myosin molecules are
tethered to a coverslip, they cannot move; thus any force generated by
interaction of myosin heads with actin filaments forces the filaments to move
relative to the myosin.

If ATP is present, added actin filaments can be seen to glide along the
surface of the coverslip; if ATP is absent, no filament movement is observed.

 This movement is caused by a

myosin head (bound to the
coverslip) walking toward the
(+) end of a filament; thus
filaments move with the (-) end
in the lead. [The one exception
is myosin VI, which moves in
the opposite direction, toward
the (-) end; so the (+) end of a
moving filament is in the lead.]
The rate at which myosin
moves an actin filament can be
determined from video camera
recordings of sliding-filament
assays.
The velocity of filament
movement can vary widely,
depending on the myosin
tested
and
the
assay
conditions (e.g., ionic strength,
ATP and Ca2+ concentrations,
temperature).

 The most critical feature of

myosin is its ability to
generate a force that powers
movements.
Researchers
have used a device called an
optical trap to measure the
forces generated by single
myosin molecules.
The results of optical-trap
studies show that myosin II
moves in discrete steps,
approximately 510 nm long,
and
generates
35
piconewtons (pN) of force,
approximately the same force
as that exerted by gravity on
a single bacterium.

Actin Myosin Motion

Figure 34.18. Myosin Motion Along Actin. A myosin head (yellow) in the
ADP form is bound to an actin filament (blue). The exchange of ADP for ATP
results in (1) the release of myosin from actin and (2) substantial
reorientation of the lever arm of myosin. Hydrolysis of ATP (3) allows the
myosin head to rebind at a site displaced along the actin filament (4). The
release of Pi (5) accompanying this binding increases the strength of
interaction between myosin and

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