Document Detail


A 29 residue region of the sarcomeric myosin rod is necessary for filament formation.
MedLine Citation:
PMID:  9047366     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Myosin is a motor protein whose functional unit in the sarcomere is the thick filament. The myosin molecule is capable of self-assembly into thick filaments through its alpha-helical coiled-coil rod domain. To define more precisely the sequence requirements for this assembly, segments of the human fast IId skeletal myosin rod were expressed in Escherichia coli and examined differential solubility and the formation of ordered paracrystals. We show that both properties appear to require a 29 residue sequence (residues 1874 to 1902) near the C terminus of the rod region. To test further the role of this region in assembly, a protein was constructed which consisted of this assembly competence domain (ACD) fused to the carboxy terminus of an assembly-incompetent myosin rod fragment. This chimeric fragment exhibited myosin's characteristic solubility properties and formed ordered paracrystals. To complement these in vitro experiments, both a full-length myosin heavy chain (MYH) and one from which the 29 residues were deleted were transfected into cultured mammalian cells. While the full-length construct formed the spindle-shaped structures characteristic of arrays of thick filaments, the deleted MYH showed only diffuse staining throughout the cytoplasm by light microscopy. Thus, there appears to be a specific sequence in the C-terminal region of the myosin heavy chain rod which is necessary for ordered paracrystal formation and is sufficient to confer assembly properties to an assembly-incompetent rod fragment.
Authors:
R L Sohn; K L Vikstrom; M Strauss; C Cohen; A G Szent-Gyorgyi; L A Leinwand
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of molecular biology     Volume:  266     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  1997 Feb 
Date Detail:
Created Date:  1997-04-04     Completed Date:  1997-04-04     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  317-30     Citation Subset:  IM    
Affiliation:
Department of Molecular, Cellular and Developmental Biology, Universityof Colorado, Boulder 80309-0347, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Binding Sites
COS Cells / metabolism
Crystallization
Escherichia coli / genetics,  metabolism
Humans
Microscopy, Electron
Models, Molecular
Molecular Sequence Data
Muscle, Skeletal / ultrastructure
Myosin Heavy Chains / chemistry,  genetics,  ultrastructure
Myosin Light Chains / chemistry,  genetics,  ultrastructure
Myosins / chemistry*,  genetics,  ultrastructure*
Protein Conformation
Recombinant Proteins / chemistry,  metabolism,  ultrastructure
Sequence Deletion
Structure-Activity Relationship
Grant Support
ID/Acronym/Agency:
AR15963/AR/NIAMS NIH HHS; GM29090/GM/NIGMS NIH HHS; T32 GM 7288/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Myosin Heavy Chains; 0/Myosin Light Chains; 0/Recombinant Proteins; EC 3.6.4.1/Myosins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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