Journal article
Leiomodin/tropomyosin interactions are isoform specific
Archives of biochemistry and biophysics, Vol.465(1), pp.227-230
2007
Handle:
https://hdl.handle.net/2376/112507
PMID: 17572376
Abstract
Leiomodins are larger homologs of tropomodulin, a tropomyosin-binding, actin-capping protein. There are several leiomodin isoforms, one of them found in smooth muscles (Lmod1) and another one found in cardiac and skeletal muscles (Lmod2). In this work, the tropomyosin-binding abilities of these two isoforms were studied. The tropomyosin-binding sites were localized in the N-terminal regions of Lmod1 and Lmod2. The affinities of the leiomodin fragments containing the tropomyosin-binding sites for tropomyosin peptides containing N-termini of different tropomyosin isoforms, α, γ and δ, were determined and compared using non-denaturing gel-electrophoresis and circular dichroism. It was shown that leiomodin/tropomyosin binding is isoform-specific and differs almost 100-fold for different tropomyosin isoforms.
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Details
- Title
- Leiomodin/tropomyosin interactions are isoform specific
- Creators
- Alla S Kostyukova - Department of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA
- Publication Details
- Archives of biochemistry and biophysics, Vol.465(1), pp.227-230
- Academic Unit
- Chemical Engineering and Bioengineering, School of
- Publisher
- Elsevier Inc
- Identifiers
- 99900548165501842
- Language
- English
- Resource Type
- Journal article