Key result
Fluorescence probing of mutant yeast actin showed that in filaments, the C-terminal pyrene of monomers directly interacts with the loop pyrene of neighboring monomers within 18 Angstroms.
Population
Yeast actin (wild-type and mutants S265C, S265C/C374A)
Comparison
Mutation of Ser265 to cysteine and Cys374 to… vs Wild-type (WT) actin
Design
Preclinical
Authors
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Extends F-actin structural models; leaves open functional roles in mammalian systems.
Fluorescence probing of yeast actin mutants reveals that the C-terminal region of monomers directly interacts with the loop between subdomains 3 and 4 of neighboring monomers in F-actin.
Feng et al. (1997) studied this question. Yeast actin mutations (S265C and S265C/C374A) with pyrene maleimide labeling vs. Wild-type (WT) actin was evaluated on Fluorescence behavior and filament formation. Fluorescence probing of mutant yeast actin showed that in filaments, the C-terminal pyrene of monomers directly interacts with the loop pyrene of neighboring monomers within 18 Angstroms.
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