Chemomechanical Transduction in the Actomyosin Molecular Motor by 2‘,3‘-Dideoxydidehydro-ATP and Characterization of Its Interaction with Myosin Subfragment 1 in the Presence and Absence of Actin†

Biochemistry ◽  
1996 ◽  
Vol 35 (31) ◽  
pp. 10149-10157 ◽  
Author(s):  
Damodaragounder Gopal ◽  
Dimitrii I. Pavlov ◽  
Dimitrii I. Levitsky ◽  
Mitsuo Ikebe ◽  
Morris Burke
Keyword(s):  
Molecular Motor ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence

Three-dimensional structure of myosin subfragment-1: a molecular motor

Science ◽  
1993 ◽  
Vol 261 (5117) ◽  
pp. 50-58 ◽  
Author(s):  
I Rayment ◽  
W. Rypniewski ◽  
K Schmidt-Base ◽  
R Smith ◽  
D. Tomchick ◽  
...  
Keyword(s):  
Molecular Motor ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Characterization of the properties of ethenoadenosine nucleotides bound or trapped at the active site of myosin subfragment 1

Biochemistry ◽  
1984 ◽  
Vol 23 (17) ◽  
pp. 3994-4002 ◽  
Author(s):  
William J. Perkins ◽  
James A. Wells ◽  
Ralph G. Yount
Keyword(s):  
Active Site ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Characterization of Myosin Subfragment-1 of Summer and Winter Silver Carp (Hypophthalmichthys molitrix) Muscle

2012 ◽  
Vol 77 (9) ◽  
pp. C914-C920 ◽  
Author(s):  
Liang Zheng ◽  
Kefeng Yu ◽  
Chunhong Yuan ◽  
Xichang Wang ◽  
Shunsheng Chen ◽  
...  
Keyword(s):  
Silver Carp ◽  
Hypophthalmichthys Molitrix ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1

Thiol-Specific Cross-Linkers of Variable Length Reveal a Similar Separation of SH1 and SH2 in Myosin Subfragment 1 in the Presence and Absence of MgADP†

Biochemistry ◽  
1999 ◽  
Vol 38 (32) ◽  
pp. 10307-10317 ◽  
Author(s):  
Werner Kliche ◽  
Jens Pfannstiel ◽  
Markus Tiepold ◽  
Stanka Stoeva ◽  
Heinz Faulstich
Keyword(s):  
Variable Length ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Presence And Absence

scholarly journals Isolation and characterization of circumferential microfilament bundles from retinal pigmented epithelial cells.

1982 ◽  
Vol 95 (1) ◽  
pp. 310-315 ◽  
Author(s):  
K Owaribe ◽  
H Masuda
Keyword(s):  
Epithelial Cells ◽  
Electrophoretic Pattern ◽  
Isolation And Characterization ◽  
Microfilament Bundles ◽  
Myosin Subfragment ◽  
Sds Page ◽  
Myosin Subfragment 1 ◽  
Retinal Pigmented Epithelial Cells ◽  
Large Contraction

Chicken retinal pigmented epithelial cells have circumferential microfilament bundles (CMBs) at the zonula adherens region. We have isolated these CMBs in intact form and characterized them structurally and biochemically. Pigmented epithelia obtained from 11-d-old chick embryos were treated with glycerol and Triton. Then, the epithelia were homogenized by passing them through syringe needles. Many isolated CMBs were found in the homogenate by phase-contrast microscopy. They formed polygons, mostly pentagons and hexagons, or fragments of polygons. Polygons were filled with meshwork structures, i.e. they were polygonal plates. Upon exposure to Mg-ATP, isolated CMBs showed clear and large contraction. The contraction was inhibited by treatment with N-ethylmaleimide-modified myosin subfragment-1. After purification by centrifugation with the density gradient of Percoll, CMBs were analyzed by SDS PAGE. The electrophoretic pattern gave three major components of 200, 55, and 42 kdaltons and several minor components. Electron microscopy showed that the polygons were composed of thick bundles of actin-containing microfilaments, and the meshworks were composed primarily of intermediate filaments.

scholarly journals Characterization of an actin-myosin head interface in the 40–113 region of actin using specific antibodies as probes

1990 ◽  
Vol 271 (2) ◽  
pp. 407-413 ◽  
Author(s):  
J P Labbé ◽  
C Méjean ◽  
Y Benyamin ◽  
C Roustan
Keyword(s):  
Myosin Head ◽  
Interface Model ◽  
Filamentous Actin ◽  
Skeletal Muscle Myosin ◽  
Myosin Subfragment ◽  
Myosin Subfragment 1 ◽  
Myosin Interaction ◽  
Muscle Myosin ◽  
Covalent Complex

Evidence for the participation of the 1-7 and 18-28 N-terminal sequences of actin at different steps of actin-myosin interaction process is well documented in the literature. Cross-linking of the rigor complex between filamentous actin and skeletal-muscle myosin subfragment 1 was accomplished by the carboxy-group-directed zero-length protein cross-linker, 1-ethyl-3-[3-(dimethylamino)propyl]carbodi-imide. After chaotropic depolymerization and thrombin digestion, which cleaves only actin, the covalent complex with Mr 100,000 was characterized by PAGE. The linkage was identified as being between myosin subfragment 1 (S-1) heavy chain and actin-(1-28)-peptide. The purified complex retained in toto its ability to combine reversibly with fresh filamentous actin, but showed a decrease in the Vmax. of actin-dependent Mg2(+)-ATPase. By using e.l.i.s.a., S-1 was observed to bind to coated monomeric actin or its 1-226 N-terminal peptide. This interaction strongly interfered with the binding of antibodies directed against the 95-113 actin sequence. Moreover, S-1 was able to bind with coated purified actin-(40-113)-peptide. Finally, antibodies directed against the 18-28 and 95-113 actin sequence, which strongly interfered with S1 binding, were unable to compete with each other. These results suggest that two topologically independent regions are involved in the actin-myosin interface: one located in the conserved 18-28 sequence and the other near residues 95-113, including the variable residue at position 89. Other experiments support the ‘multisite interface model’, where the two actin sites could modulate each other during S-1 interaction.

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