scholarly journals Exploring the Effects of Mutations and Thick Filament Proteins on Myofilament Calcium Kinetics Via Stopped-Flow

2021 ◽  
Vol 120 (3) ◽  
pp. 54a-55a
Author(s):  
Matthew M. Klass ◽  
Rhye-Samuel Kanassatega ◽  
Sarah Lehman ◽  
Jil C. Tardiff ◽  
Brett A. Colson ◽  
...  
2020 ◽  
Vol 118 (3) ◽  
pp. 327a
Author(s):  
Matthew M. Klass ◽  
Grace Heffernon ◽  
Garrett Hauck ◽  
Sarah Lehman ◽  
Jonathan P. Davis ◽  
...  

Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.


1986 ◽  
Vol 47 (C8) ◽  
pp. C8-555-C8-561 ◽  
Author(s):  
S. SAIGO ◽  
H. OYANAGI ◽  
T. MATSUSHITA ◽  
H. HASHIMOTO ◽  
N. YOSHIDA ◽  
...  

Genetics ◽  
2000 ◽  
Vol 156 (2) ◽  
pp. 631-643
Author(s):  
Pamela E Hoppe ◽  
Robert H Waterston

Abstract The precise arrangement of molecules within the thick filament, as well as the mechanisms by which this arrangement is specified, remains unclear. In this article, we have exploited a unique genetic interaction between one isoform of myosin heavy chain (MHC) and paramyosin in Caenorhabditis elegans to probe the molecular interaction between MHC and paramyosin in vivo. Using chimeric myosin constructs, we have defined a 322-residue region of the MHC A rod critical for suppression of the structural and motility defects associated with the unc-15(e73) allele. Chimeric constructs lacking this region of MHC A either fail to suppress, or act as dominant enhancers of, the e73 phenotype. Although the 322-residue region is required for suppression activity, our data suggest that sequences along the length of the rod also play a role in the isoform-specific interaction between MHC A and paramyosin. Our genetic and cell biological analyses of construct behavior suggest that the 322-residue region of MHC A is important for thick filament stability. We present a model in which this region mediates an avid interaction between MHC A and paramyosin in parallel arrangement in formation of the filament arms.


RSC Advances ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 1086-1097
Author(s):  
Shunki Takaramoto ◽  
Yusuke Nakasone ◽  
Kei Sadakane ◽  
Shinsaku Maruta ◽  
Masahide Terazima

Dynamics of conformation changes of α-synuclein induced by the presence of SDS micelles are revealed using time-resolved diffusion, CD, and FRET measurements combined with a micro-stopped flow system.


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