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Home / Equine Research Bank / Mol Cell Biochem / Structural and functional properties of the non-muscle tropo...
Molecular and cellular biochemistry1983; 57(2); 127-146; doi: 10.1007/BF00849190

Structural and functional properties of the non-muscle tropomyosins.

Abstract: The non-muscle tropomyosins (TMs), isolated from such tissues as platelets, brain and thyroid, are structurally very similar to the muscle TMs, being composed of two highly alpha-helical subunits wound around each other to form a rod-like molecule. The non-muscle TMs are shorter than the muscle TMs; sequence analysis demonstrates that each subunit of equine platelet TM consists of 247 amino acids, 37 fewer than for skeletal muscle TM. The major differences in sequence between platelet and skeletal muscle TM are found near the amino and carboxyl terminal ends of the proteins. Probably as the result of such alterations, the non-muscle TMs aggregate in a linear end-to-end manner much more weakly than do the muscle TMs. Since end-to-end interactions are responsible for the highly cooperative manner in which TM binds to actin, the non-muscle TMs have a lower affinity for actin filaments than do the muscle TMs. However, the attachment of other proteins to actin (e.g. the Tn-I subunit of skeletal muscle troponin or the S-1 subfragment of skeletal muscle myosin) can increase the affinity of actin filaments for non-muscle TM. The non-muscle TMs interact functionally with the Tn-I component of skeletal muscle troponin to inhibit the ATPase activity of muscle actomyosin and with whole troponin to regulate the muscle actomyosin ATPase in a Ca++-dependent manner, even though one of the binding sites for troponin on skeletal TM is missing in non-muscle TM. A novel actomyosin regulatory system can be produced using Tn-I, calmodulin and non-muscle TM; in this case inhibition is released when the non-muscle TM detaches from the actin filament in the presence of Ca++. Although it has not yet been demonstrated that the non-muscle TMs participate in a Ca++-dependent contractile regulatory system in vivo it does appear that they are associated with actin filaments in vivo.
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Publication Date: 1983-01-01 PubMed ID: 6361516DOI: 10.1007/BF00849190Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article explores the structural and functional properties of non-muscle tropomyosins (TMs) found in tissues like platelets, brain, and thyroid, comparing them with muscle TMs. It portrays non-muscle TMs as shorter, sequencing and functional differences, particularly in their interaction with actin filaments and ATPase activity regulation.

Structural Differences

  • The researchers identify a structural similarity between non-muscle and muscle TMs as rod-like molecules arising from two highly alpha-helical subunits coiled together. However, non-muscle TMs are smaller, the study showing that each subunit of equine platelet TM has 247 amino acids, 37 less than skeletal muscle TMs.
  • The key sequencing variations between platelet and skeletal muscle TM occur near the proteins’ amino and carboxyl terminal ends. Such alterations seemingly cause non-muscle TMs to aggregate in a linear end-to-end format with less robustness than muscle TMs.

Functional Differences

  • The study suggests that due to their end-to-end interactions facilitating TM’s cooperative tie to actin, non-muscle TMs exhibit a reduced affinity for actin filaments as opposed to muscle TMs. However, they note that when other proteins (e.g., the Tn-I subunit of skeletal muscle troponin or the S-1 subfragment of skeletal muscle myosin) attach to actin, the affinity of actin filaments for non-muscle TM can increase.
  • Despite one of the troponin binding sites on skeletal TM missing on non-muscle TM, non-muscle TMs interact functionally with the Tn-I component of skeletal muscle troponin. This interaction inhibits the ATPase activity of muscle actomyosin while regulating muscle actomyosin ATPase in a Ca++-dependent approach.
  • The researchers also described a unique actomyosin regulatory method using Tn-I, calmodulin, and non-muscle TM, which releases inhibition when the non-muscle TM detaches from the actin filament in Ca++ presence.

Non-Muscle TM Association with Actin Filaments In Vivo

  • While the study doesn’t establish whether non-muscle TMs participate in a Ca++-dependent contractile regulatory system in vivo, the evidence suggests they are linked with actin filaments in vivo.

Cite This Article

APA
Côté GP. (1983). Structural and functional properties of the non-muscle tropomyosins. Mol Cell Biochem, 57(2), 127-146. https://doi.org/10.1007/BF00849190

Publication

Molecular and cellular biochemistry
ISSN: 0300-8177
NlmUniqueID: 0364456
Country: Netherlands
Language: English
Volume: 57
Issue: 2
Pages: 127-146

Researcher Affiliations

Côté, G P

    MeSH Terms

    • Amino Acid Sequence
    • Amino Acids / analysis
    • Animals
    • Blood Platelets / analysis
    • Brain Chemistry
    • Cattle
    • Chickens
    • Fibroblasts / analysis
    • Horses
    • Humans
    • Molecular Weight
    • Muscles / analysis
    • Protein Conformation
    • Rabbits
    • Species Specificity
    • Swine
    • Thyroid Gland / analysis
    • Tissue Distribution
    • Tropomyosin / analysis
    • Troponin / analysis

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