ArticleBiophysical journal2001
Tryptophan fluorescence of yeast actin resolved via conserved mutations.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Myofilamental integrity of the myometrium due to cold ischaemia stress during autotransplantation in the experimental sheep model.PloS one · 2025Article
- Interactions between Quantum Dots and G-Actin.International journal of molecular sciences · 2023Article
- Two Deafness-Causing Actin Mutations (DFNA20/26) Have Allosteric Effects on the Actin Structure.Biophysical journal · 2016Article
- Flavonoids affect actin functions in cytoplasm and nucleus.Biophysical journal · 2007Article
- Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii.Molecular biology of the cell · 2006Article
- Characterization of f-actin tryptophan phosphorescence in the presence and absence of tryptophan-free myosin motor domain.Biophysical journal · 2004Article
- Functional studies of yeast actin mutants corresponding to human cardiomyopathy mutations.Journal of muscle research and cell motility · 2001Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Actin contains four tryptophan residues, W79, W86, W340, and W356, all located in subdomain 1 of the protein. Replacement of each of these residues with either tyrosine (W79Y and W356Y) or phenylalanine (W86F and W340F) generated viable proteins in the yeast Saccharomyces cerevisiae, which, when purified, allowed the analysis of the contribution of these residues to the overall tryptophan fluorescence of actin. The sum of the relative contributions of these tryptophans was found to account for the intrinsic fluorescence of wild-type actin, indicating that energy transfer between the tryptophans is not the main determinant of their quantum yield, and that these mutations induce little conformational change to the protein. This was borne out by virtually identical polymerization rates and similar myosin interactions of each of the mutants and the wild-type actin. In addition, these mutants allowed the dissection of the microenvironment of each tryptophan as actin undergoes conformational changes upon metal cation exchange and polymerization. Based on the relative tryptophan contributions determined from single mutants, a triple mutant of yeast actin (W79) was generated that showed small intrinsic fluorescence and should be useful for studies of actin interactions with actin-binding proteins.
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