Cross-Bridge Number, Position, and Angle in Target Zones of Cryofixed Isometrically Active Insect Flight Muscle
Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7 nm. To quantify the parameters that govern this pattern, we measure...
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Published in | Biophysical journal Vol. 86; no. 5; pp. 3009 - 3019 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Elsevier Inc
01.05.2004
Biophysical Society The Biophysical Society |
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Abstract | Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7
nm. To quantify the parameters that govern this pattern, we measured the number and position of attached myosin heads by tracing cross-bridges through the three-dimensional tomogram from their origins on 14.5-nm-spaced shelves along the thick filament to their thin filament attachments in the target zones. The relationship between the probability of cross-bridge formation and axial offset between the shelf and target zone center was well fitted by a Gaussian distribution. One head of each myosin whose origin is close to an actin target zone forms a cross-bridge most of the time. The probability of cross-bridge formation remains high for myosin heads originating within 8
nm axially of the target zone center and is low outside 12
nm. We infer that most target zone cross-bridges are nearly perpendicular to the filaments (60% within 11°). The results suggest that in isometric contraction, most cross-bridges maintain tension near the beginning of their working stroke at angles near perpendicular to the filament axis. Moreover, in the absence of filament sliding, cross-bridges cannot change tilt angle while attached nor reach other target zones while detached, so may cycle repeatedly on and off the same actin target monomer. |
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AbstractList | Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7 nm. To quantify the parameters that govern this pattern, we measured the number and position of attached myosin heads by tracing cross-bridges through the three-dimensional tomogram from their origins on 14.5-nm-spaced shelves along the thick filament to their thin filament attachments in the target zones. The relationship between the probability of cross-bridge formation and axial offset between the shelf and target zone center was well fitted by a Gaussian distribution. One head of each myosin whose origin is close to an actin target zone forms a cross-bridge most of the time. The probability of cross-bridge formation remains high for myosin heads originating within 8 nm axially of the target zone center and is low outside 12 nm. We infer that most target zone cross-bridges are nearly perpendicular to the filaments (60% within 11 degrees ). The results suggest that in isometric contraction, most cross-bridges maintain tension near the beginning of their working stroke at angles near perpendicular to the filament axis. Moreover, in the absence of filament sliding, cross-bridges cannot change tilt angle while attached nor reach other target zones while detached, so may cycle repeatedly on and off the same actin target monomer. Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7 nm. To quantify the parameters that govern this pattern, we measured the number and position of attached myosin heads by tracing cross-bridges through the three-dimensional tomogram from their origins on 14.5-nm-spaced shelves along the thick filament to their thin filament attachments in the target zones. The relationship between the probability of cross-bridge formation and axial offset between the shelf and target zone center was well fitted by a Gaussian distribution. One head of each myosin whose origin is close to an actin target zone forms a cross-bridge most of the time. The probability of cross-bridge formation remains high for myosin heads originating within 8 nm axially of the target zone center and is low outside 12 nm. We infer that most target zone cross-bridges are nearly perpendicular to the filaments (60% within 11°). The results suggest that in isometric contraction, most cross-bridges maintain tension near the beginning of their working stroke at angles near perpendicular to the filament axis. Moreover, in the absence of filament sliding, cross-bridges cannot change tilt angle while attached nor reach other target zones while detached, so may cycle repeatedly on and off the same actin target monomer. Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7 nm. To quantify the parameters that govern this pattern, we measured the number and position of attached myosin heads by tracing cross-bridges through the three-dimensional tomogram from their origins on 14.5-nm-spaced shelves along the thick filament to their thin filament attachments in the target zones. The relationship between the probability of cross-bridge formation and axial offset between the shelf and target zone center was well fitted by a Gaussian distribution. One head of each myosin whose origin is close to an actin target zone forms a cross-bridge most of the time. The probability of cross-bridge formation remains high for myosin heads originating within 8 nm axially of the target zone center and is low outside 12 nm. We infer that most target zone cross-bridges are nearly perpendicular to the filaments (60% within 11°). The results suggest that in isometric contraction, most cross-bridges maintain tension near the beginning of their working stroke at angles near perpendicular to the filament axis. Moreover, in the absence of filament sliding, cross-bridges cannot change tilt angle while attached nor reach other target zones while detached, so may cycle repeatedly on and off the same actin target monomer. [PUBLICATION ABSTRACT] Electron micrographic tomograms of isometrically active insect flight muscle, freeze substituted after rapid freezing, show binding of single myosin heads at varying angles that is largely restricted to actin target zones every 38.7 nm. To quantify the parameters that govern this pattern, we measured the number and position of attached myosin heads by tracing cross-bridges through the three-dimensional tomogram from their origins on 14.5-nm-spaced shelves along the thick filament to their thin filament attachments in the target zones. The relationship between the probability of cross-bridge formation and axial offset between the shelf and target zone center was well fitted by a Gaussian distribution. One head of each myosin whose origin is close to an actin target zone forms a cross-bridge most of the time. The probability of cross-bridge formation remains high for myosin heads originating within 8 nm axially of the target zone center and is low outside 12 nm. We infer that most target zone cross-bridges are nearly perpendicular to the filaments (60% within 11°). The results suggest that in isometric contraction, most cross-bridges maintain tension near the beginning of their working stroke at angles near perpendicular to the filament axis. Moreover, in the absence of filament sliding, cross-bridges cannot change tilt angle while attached nor reach other target zones while detached, so may cycle repeatedly on and off the same actin target monomer. |
Author | Goldman, Yale E. Winkler, Hanspeter Franzini-Armstrong, Clara Reedy, Michael K. Sasaki, Hiroyuki Tregear, Richard T. Lucaveche, Carmen Taylor, Kenneth A. Reedy, Mary C. |
AuthorAffiliation | Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom; † Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 USA; ‡ Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19194-6083 USA; § Institute of Molecular Biophysics, Florida State University, Florida 32306-4380 USA; ¶ Institute of DNA Medicine, Jikei University School of Medicine, 3-25-8 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Japan |
AuthorAffiliation_xml | – name: Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom; † Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 USA; ‡ Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19194-6083 USA; § Institute of Molecular Biophysics, Florida State University, Florida 32306-4380 USA; ¶ Institute of DNA Medicine, Jikei University School of Medicine, 3-25-8 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Japan |
Author_xml | – sequence: 1 givenname: Richard T. surname: Tregear fullname: Tregear, Richard T. email: rt1@mrc-lmb.cam.ac.uk organization: Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 2QH, United Kingdom – sequence: 2 givenname: Mary C. surname: Reedy fullname: Reedy, Mary C. organization: Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 USA – sequence: 3 givenname: Yale E. surname: Goldman fullname: Goldman, Yale E. organization: Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19194-6083 USA – sequence: 4 givenname: Kenneth A. surname: Taylor fullname: Taylor, Kenneth A. organization: Institute of Molecular Biophysics, Florida State University, Florida 32306-4380 USA – sequence: 5 givenname: Hanspeter surname: Winkler fullname: Winkler, Hanspeter organization: Institute of Molecular Biophysics, Florida State University, Florida 32306-4380 USA – sequence: 6 givenname: Clara surname: Franzini-Armstrong fullname: Franzini-Armstrong, Clara organization: Pennsylvania Muscle Institute, University of Pennsylvania, Philadelphia, Pennsylvania 19194-6083 USA – sequence: 7 givenname: Hiroyuki surname: Sasaki fullname: Sasaki, Hiroyuki organization: Institute of DNA Medicine, Jikei University School of Medicine, 3-25-8 Nishi-shinbashi, Minato-ku, Tokyo 105-8461, Japan – sequence: 8 givenname: Carmen surname: Lucaveche fullname: Lucaveche, Carmen organization: Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 USA – sequence: 9 givenname: Michael K. surname: Reedy fullname: Reedy, Michael K. organization: Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710 USA |
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SubjectTerms | Actins - chemistry Actins - metabolism Adenosine Triphosphate - chemistry Animals Calcium - metabolism Cellular biology Flight, Animal Hemiptera Image Processing, Computer-Assisted Kinetics Microscopy, Electron Muscle Contraction Muscle Fibers, Skeletal - cytology Muscles - metabolism Muscles and Contractility Muscular system Myosin Subfragments - chemistry Myosins - chemistry Normal Distribution Proteins |
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Title | Cross-Bridge Number, Position, and Angle in Target Zones of Cryofixed Isometrically Active Insect Flight Muscle |
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