May 1, 1992Journal of Biological ChemistryOpen Access

Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo.

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Population

Saccharomyces cerevisiae actin (wild type and mutants DNEQ and delta DSE)

Comparison

Site-directed mutagenesis vs Wild type yeast actin

Design

Preclinical

Authors

RCR.K. CookOklahoma State University WBW.T. BlakeUniversity of Iowa PRPeter A. RubensteinUniversity of Iowa

Discussion

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Implication

Yeast actin NH2-terminal mutants remain viable despite bundling and myosin defects; leaves open translation to human actinopathies or cardiac function.

Structured PICO

Population

Saccharomyces cerevisiae actin (wild type and mutants DNEQ and delta DSE)

Intervention

Site-directed mutagenesis (DNEQ actin and delta DSE actin)

Comparator

Wild type yeast actin

Outcome

Actin function in vitro (peptide mapping, filament bundling, ATPase activity activation) and in vivo (ability to support secretion)surrogate

Removal of NH2-terminal negative charges in yeast actin promotes filament bundling and slightly impairs secretion and myosin S1 ATPase activation, though not essential for viability.

Cite This Study

Cook et al. (1992) studied this question.

synapsesocial.com/papers/6a787d45e29fd788c9f804fb https://doi.org/10.1016/s0021-9258(19)50441-0

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Implication

Yeast actin NH2-terminal mutants remain viable despite bundling and myosin defects; leaves open translation to human actinopathies or cardiac function.

Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Removal of the amino-terminal acidic residues of yeast actin. Studies in vitro and in vivo.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider