Actin from Saccharomyces cerevisiae.

Greer, Chris L.; Schekman, Randy

doi:10.1128/mcb.2.10.1270

Cited by 65 publications

(49 citation statements)

References 42 publications

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“…As reported earlier, this behaviour is restricted to non-muslce actins [40], with yeast actin showing the most dramatic difference compared to muscle actin [41]. Greer and Schekman [42] showed that yeast actin tends to aggregate in the presence of Ca2+, and observations of the Ca2 + influence on the polymerization of bovine p-actin implicate the presence of an additional, lowaffinity Ca2+-binding site on p-actin compared to a-actin [43].…”

Section: Resultsmentioning

confidence: 76%

Interference with myosin subfragment‐1 binding by site‐directed mutagenesis of actin

Aspenström

Karlsson

1991

European Journal of Biochemistry

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Three N‐terminal double mutants of β‐actin expressed in the yeast Saccharomyces cerevisiae have been characterized with respect to DNase‐I interaction, N‐terminal post‐translational modification, polymerizability and myosin subfragment‐1 binding. The results strongly support earlier suggestions that the acidic residues at the N‐terminus of actin are part of the myosin‐binding site, while they seem to be of no importance for the other aspects of actin biochemistry tested. The suitability of this expression system for production of recombinant actin in general is discussed.

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Section: Resultsmentioning

confidence: 76%

Interference with myosin subfragment‐1 binding by site‐directed mutagenesis of actin

Aspenström

Karlsson

1991

European Journal of Biochemistry

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“…Profilin and myosin II of D. discoideum show different affinities for actin from various sources (Greer and Schekman, 1982;Haugwitz et al, 1991), but Dd plastin is the first protein known from this organism that does not bind actin from rabbit skeletal muscle to any significant extent. The protein appears therefore to bind to a region where the major actin (actin 15) of D. discoideum (Vandekerckhove and Weber, 1980) differs in its structure from rabbit a-actin.…”

Section: Distribution Of Dd Plastin In Cells Of Different Developmentmentioning

confidence: 99%

Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.

Prassler

Stöcker

Marriott

et al. 1997

MBoC

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A protein purified from cytoskeletal fractions of Dictyostelium discoideum proved to be a member of the fimbrin/plastin family of actin-bundling proteins. Like other family members, this Ca2+-inhibited 67-kDa protein contains two EF hands followed by two actin-binding sites of the a-actinin/ 3-spectrin type. Dd plastin interacted selectively with actin isoforms: it bound to D. discoideum actin and to 0/y-actin from bovine spleen but not to a-actin from rabbit skeletal muscle. Immunofluorescence labeling of growth phase cells showed accumulation of Dd plastin in cortical structures associated with cell surface extensions. In the elongated, streaming cells of the early aggregation stage, Dd plastin was enriched in the front regions. To examine how the bundled actin filaments behave in myosin II-driven motility, complexes of F-actin and Dd plastin were bound to immobilized heavy meromyosin, and motility was started by photoactivating caged ATP. Actin filaments were immediately propelled out of bundles or even larger aggregates and moved on the myosin as separate filaments. This result shows that myosin can disperse an actin network when it acts as a motor and sheds light on the dynamics of proteinprotein interactions in the cortex of a motile cell where myosin II and Dd plastin are simultaneously present.

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“…It contains a single essential actin gene (ACT1), and easy genetic manipulation allows the ready exchange of a mutant actin gene for its wild-type counterpart. Its actin is about 90% identical in amino acid sequence to the mammalian cytoskeletal actins and about 87% identical to the striated muscle actins [Greer and Schekman, 1982;Ng et al, 1985]. Its actin cytoskeleton contains many of the same proteins as do mammalian cells, and robust methods have been established for assessing in vivo cytoskeleton function in yeast using a combination of genetics and microscopy.…”

Section: Budding Yeast As An Expression System For Mutant Actinsmentioning

confidence: 99%

Insights into the effects of disease‐causing mutations in human actins

Rubenstein

Wen

2014

Cytoskeleton

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Mutations in all six actins in humans have now been shown to cause diseases. However, a number of factors have made it difficult to gain insight into how the changes in actin functions brought about by these pathogenic mutations result in the disease phenotype. These include the presence of multiple actins in the same cell, limited accessibility to pure mutant material, and complexities associated with the structures and their component cells that manifest the diseases. To try to circumvent these difficulties, investigators have turned to the use of model systems. This review describes these various approaches, the initial results obtained using them, and the insight they have provided into allosteric mechanisms that govern actin function. Although results so far have not explained a particular disease phenotype at the molecular level, they have provided valuable insight into actin function at the mechanistic level which can be utilized in the future to delineate the molecular bases of these different actinopathies. Key Words: actin; allostery; disease; mutation; isoforms Introduction A ctin mutations can cause human disease. However, little is known concerning the mechanisms by which these mutations lead to the disease phenotypes they produce. The goal of this review is to describe the general properties of actin, the diseases associated with mutations in actin, methodologies that might be employed to achieve a mechanistic understanding of actin based disease and efforts that have been made toward this goal. Properties of G-and F-ActinA discussion of the effects of pathogenic mutations on actin function requires a basic understanding of actin structure and its solution properties. Actin is an abundant 42 kD monomeric protein, found in virtually all eukaryotic cells, that can cycle between either a monomeric (G-actin) or polymeric (F-actin) state. It plays both contractile and structural roles in the cytoplasm, and recent studies have documented that actin in the nucleus acts as a promoter of transcription or as a member of a number of chromatin remodeling complexes Philimonenko et al., 2004;Miyamoto and Gurdon, 2011; Miyamoto et al., 2011a,b;Weston et al., 2012].G-actin is a clam-shaped protein with two domains, the inner and outer domains ( Fig. 1), connected by a hinge region, and separated by a deep cleft. Outer (subdomains 1 and 2) and inner (subdomains 3 and 4) refer to their position in the actin filament. The N and C-termini reside on opposite faces of the protein in subdomain 1. An adenine nucleotide binds deep within the inter-domain cleft, held in place by a divalent cation, and imparts stability to the protein and the filament. This latter role depends on its ability to cycle between the ATP and ADP state by virtue of a polymerization-dependent ATPase activity [Carlier et al., 1987;Korn et al., 1987]. F-actin is a polar structure with pointed (2) and barbed (1) ends referring to the arrowhead pattern formed when myosin S1 binds to F-actin in the absence of ATP [Craig et al., 1985]. The polarity of th...

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Actin from Saccharomyces cerevisiae.

Cited by 65 publications

References 42 publications

Interference with myosin subfragment‐1 binding by site‐directed mutagenesis of actin

Interference with myosin subfragment‐1 binding by site‐directed mutagenesis of actin

Interaction of a Dictyostelium member of the plastin/fimbrin family with actin filaments and actin-myosin complexes.

Insights into the effects of disease‐causing mutations in human actins

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