Document Detail


N-terminal modification and its effect on the biochemical characteristics of Akazara scallop tropomyosins expressed in Escherichia coli.
MedLine Citation:
PMID:  15269246     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Akazara scallop striated muscle tropomyosin mutants without a fused amino acid (nf-Tm), and with Ala- (A-Tm) or Asp-Ala- (DA-Tm) fused at the N-terminus were expressed in Escherichia coli cells. Among them, nf-Tm alone has an initial methionine. The native Akazara scallop tropomyosin and DA-Tm showed similar alpha-helix contents and intrinsic viscosity, but nf-Tm and A-Tm exhibited lower values than those of the native tropomyosin. According to the relative viscosity, all the expressed tropomyosins appear to have lost head-to-tail polymerization ability. Though nf-Tm has extremely low actin-binding ability, the ability was almost completely recovered with a two amino acid fusion but incompletely with a one amino acid fusion. On the other hand, an amino acid fusion, irrespective of the number, seemed to inhibit the Mg-ATPase activity of actomyosin. However, the bacterially expressed tropomyosins together with Akazara scallop troponin do not confer the full Ca(2+)-regulation ability of Mg-ATPase activity of actomyosin. These results support that N-terminal blocking probably by an acetyl group of Akazara scallop tropomyosin plays an important role not only in head-to-tail polymerization and actin-binding, as known for vertebrate tropomyosin, but also in maintaining the secondary or higher structure and Ca(2+)-regulation together with troponin.
Authors:
Akira Inoue; Takao Ojima; Kiyoyoshi Nishita
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of biochemistry     Volume:  136     ISSN:  0021-924X     ISO Abbreviation:  J. Biochem.     Publication Date:  2004 Jul 
Date Detail:
Created Date:  2004-07-22     Completed Date:  2004-09-23     Revised Date:  2007-12-19    
Medline Journal Info:
Nlm Unique ID:  0376600     Medline TA:  J Biochem     Country:  Japan    
Other Details:
Languages:  eng     Pagination:  107-14     Citation Subset:  IM    
Affiliation:
Laboratory of Biochemistry and Biotechnolgy, Graduate School of Fisheries Sciences, Hokkaido University, Hakodate 041-8611.
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MeSH Terms
Descriptor/Qualifier:
Actins / metabolism
Amino Acid Sequence
Animals
Base Sequence
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Molecular Sequence Data
Mollusca / chemistry*,  genetics,  metabolism
Mutation
Temperature
Tropomyosin / chemistry*,  genetics,  metabolism
Chemical
Reg. No./Substance:
0/Actins; 0/Tropomyosin

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