Foerster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1

Dalbey, Ross E.; Weiel, Jurgen; Yount, Ralph G.

doi:10.1021/bi00289a014

Cited by 76 publications

(67 citation statements)

References 65 publications

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“…That bound nucleotide enters a "pocket" is also shown by the observations of Ando et al (65). Moreover, Yount and co-workers (16) and Cheung and co-workers (66) have shown that as the nucleotide initiates the pocket formation the distance between Cys-697 and Cys-707 decreases. However, in this decrease the two thiols may move unsymmetrically.…”

Section: Structural Information Of Other Kindsmentioning

confidence: 66%

On the origin and transmission of force in actomyosin subfragment 1.

Botts

Thomason

Morales

1989

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

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A proximity map showing the three-dimensional arrangement of 12 chemically defined points in actomyosin subfragment 1 is developed and roughly correlated with published electron microscope reconstructions of others. Several additional points and topological relationships in the primary polypeptide chain folding are assimilated into this model. Certain crossliikings and distance change observations are interpreted as indicators of transmission of force/displacement between the nucleotide-binding and an actin-binding site-i.e., as indications of how energy is transduced in this system.It is reasonable to think that contractile force arises because the equilibrium geometrical relations between actin and the subfragment 1 (S-1) segment of myosin are different for each enzymatic intermediate occupying an ATPase site of S-1 that is remote from the (S-1)-actin interface(s). Then the operation of the enzymatic cycle compels operation of a cycle of relations between S-1 and actin. If changes in these relations are resisted by (surmountable) external forces, the cycle of relations is a "work cycle" performing external work. In a repetitive system, chemical free energy is thus continuously transduced into mechanical work. One has to say how the binding of an enzymatic intermediate determines an actinbinding relation 5 nm away. We have suggested that binding of the intermediate at the ATPase distorts the local S-1 structure and that this distortion is mechanically transmitted to the distant actin-binding site. These ideas have been developed in previous papers (1-3). This paper fleshes out such ideas with recent observations. Structural Information froin Fluorescence Resonance Energy Transfer (FRET) Mapping and Electron Microscopy (EM)We begin by exploring the structure that may transmit effects between the nucleotide-binding site (N site) and the actinbinding site(s) (A site).A Since crystallography is still unavailable, we resort to melding lesser methods. As shown previously, chemically defined points in acto-(S-1) can be pairwise labeled by fluorophores. From FRET between such a pair one can estimate the interpoint distance, and by repetition of the procedure one can build up a lattice of acto-(S-1) points (2, 5). The improvement offered by the Dale et al. (6) analysis was previously incorporated (2, 7), but since 1984, other developments have appeared (see below). Though we cite improvements we must also emphasize the limitations of proximity mapping inherent in our results. For example, every point lattice has at least one unresolvable "mirror image" ambiguity. More serious is a shortage of necessary distance measurements. Although n(n -1)/2 distances are displayed in a complete lattice of n points, only 4n -10 distances are required to construct the lattice (2). But in our case even this smaller number has not yet been obtained. The missing distances have been assigned by using extraneous information of variable reliability. For example, chemical information may favor the proximity of two points, sequence loc...

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Section: Structural Information Of Other Kindsmentioning

confidence: 66%

On the origin and transmission of force in actomyosin subfragment 1.

Botts

Thomason

Morales

1989

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

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“…It is expected that any other residue in this latter location would alter the conformation of this segment and change the domain-domain interactions. Chemical and structural studies of myosin have indicated that there must be a significant structural rearrangement associated with the reactive sulffihydryl groups during the contractile cycle (38)(39)(40)(41). In the structure of chicken skeletal myosin Si, these two residues are separated by an a-helix where their side chains point in opposite directions (23), yet they can be cross-linked in the presence of nucleotide (42)(43)(44) and chemical modification of the cysteines changes the kinetic properties of myosin (45,46).…”

Section: Resultsmentioning

confidence: 99%

Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy.

Rayment

Holden

Sellers

et al. 1995

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

212

142

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In 10-30% of hypertrophic cardiomyopathy kindreds, the disease is caused by >29 missense mutations in the cardiac f8-myosin heavy chain (AYIH7) gene. The amino acid sequence similarity between chicken skeletal muscle and human a-cardiac myosin and the three-dimensional structure of the chicken skeletal muscle myosin head have provided the opportunity to examine the structural consequences of these naturally occurring mutations in human ,8-cardiac myosin. This study demonstrates that the mutations are related to distinct structural and functional domains. Twenty-four are clustered around four specific locations in the myosin head that are (i) associated with the actin binding interface, (ii) around the nucleotide binding site, (iii) adjacent to the region that connects the two reactive cysteine residues, and (iv) in close proximity to the interface of the heavy chain with the essential light chain. The remaining five mutations are in the myosin rod. The locations of these mutations provide insight into the way they impair the functioning of this molecular motor and also into the mechanism of energy transduction.

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“…, where the values of R o Ј and d Ј were reported to be 29.0 Å and 20.6 ns, respectively, by Dalbey et al (1983). R is the donor-acceptor separation distance, R ϭ R o (E Ϫ1 Ϫ 1) decay of C2 DAN /C155 contains primarily a nondecaying component, consistent with the fact that the majority of the RLCs are bound to MHC with a rotational relaxation time that is too long to be measured.…”

Section: Fluorescence Polarization Measurements Of Dan-labeled Mutantmentioning

confidence: 87%

Proximity Relationships between Engineered Cysteine Residues in Chicken Skeletal Myosin Regulatory Light Chain:

Wolff-Long

Tao

Lowey

1995

Journal of Biological Chemistry

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Resonance energy transfer was used to measure the distances between pairs of cysteines, Cys 2 and Cys 155and Cys 73 and Cys 155, in recombinant chicken skeletal myosin regulatory light chains in the free and bound states. The fluorescent and nonfluorescent probes N-iodoacetyl-N-(5-sulfo-1-naphthyl)ethylenediamine and N-(4-dimethylamino-3,5-dinitrophenyl)maleimide were used as the donor and the acceptor, respectively. The distance between Cys 2 and Cys 155 was measured to be 35 and 30 Å in the absence and presence of myosin heavy chain, respectively, suggesting a slightly more compact structure for the light chain in the bound state. The distance between Cys 73 and Cys 155 measured in a similar manner was 31 and 30 Å in the free and bound states, respectively; this latter value is in good agreement with that derived from crystallographic structures. For heavy chain-bound light chains, no measurable distance changes were detected with the binding of ATP or actin. These results show that no gross structural changes occur within the regulatory light chain during the contraction cycle, but that resonance energy transfer between other sites could be used to monitor potential changes in the myosin head upon the binding of nucleotides and actin.Force generation in muscle results from a cyclic interaction of the myosin head (S1) 1 with actin. It is currently believed that S1 may change its orientation relative to the actin filament during this process and thereby produce a displacement of ϳ50 -100 Å, the so-called "working stroke" (Huxley, 1969;Huxley and Simmons, 1971). A persistent problem with the "rotating cross-bridge model" has been the failure to detect any large conformational change in the head by most biophysical methods. It has been suggested that the reactive Cys 707 on the heavy chain, the site of labeling for most spectroscopic probes, may not be particularly sensitive to angular changes, and the portion of S1 adjacent to the rod might undergo more pronounced structural changes during hydrolysis (Huxley and Kress, 1985). We have therefore focused our efforts over the last few years on preparing Cys mutants of the regulatory light chain (RLC), a subunit which is readily exchanged into myosin, and can therefore provide a means to introduce probes into the COOH-terminal region of the myosin head (Saraswat and Lowey, 1991;Saraswat et al., 1992). Moreover, this approach avoids modification of the reactive heavy chain Cys residues, SH1 and SH2, which can have adverse effects on the enzymatic activity and motor properties of myosin (Root and Reisler, 1992).Several earlier studies have used labeled light chains to detect structural changes in the myosin head. By incorporating a 1,5-IAEDANS-labeled RLC into smooth muscle myosin, Morita et al. (1991) were able to show by fluorescence anisotropy that a change in conformation at the head/rod junction can be correlated with the transition from a folded to an extended myosin molecule. Hambly et al. (1991) exchanged a spin-labeled light chain into skinned skeletal muscle ...

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Foerster energy transfer measurements of thiol 1 to thiol 2 distances in myosin subfragment 1

Cited by 76 publications

References 65 publications

On the origin and transmission of force in actomyosin subfragment 1.

On the origin and transmission of force in actomyosin subfragment 1.

Structural interpretation of the mutations in the beta-cardiac myosin that have been implicated in familial hypertrophic cardiomyopathy.

Proximity Relationships between Engineered Cysteine Residues in Chicken Skeletal Myosin Regulatory Light Chain:

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