Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions.

Drees, Becky; Brown, Cory N.; Barrell, Barclay G.; Bretscher, Anthony

doi:10.1083/jcb.128.3.383

Cited by 133 publications

(168 citation statements)

References 42 publications

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“…The most likely candidate for a second Mdm20-dependent acetylation substrate is Tpm2p, the minor form of tropomyosin in budding yeast. Combinations of tpm1 and tpm2 mutations are also synthetically lethal in yeast (5). Thus, a tpm1 tpm2 genotype may effectively mimic the situation in which a tpm1 mdm20 cell finds itself, having no Tpm1p and only unacetylated, crippled Tpm2p.…”

Section: Discussionmentioning

confidence: 99%

“…Whole-cell protein lysates of JSY999 and JSY3315 were separated by electrophoresis on an SDS͞12% polyacrylamide gel, transferred to nitrocellulose, and processed for Western blotting by using standard methods (20). Tpm1-5p, Tpm1p, and Tpm2p were recognized by using a rabbit polyclonal antiserum, B43 (1:3,000) (5,29), with cross-reactivity to all three proteins (provided by A. Bretscher, Cornell University, Ithaca, NY). Detection was carried out by using a monoclonal horseradish peroxidaseconjugated goat anti-rabbit secondary antibody (1:50,000) (Jackson ImmunoResearch) and the enhanced chemiluminescence kit (New England Nuclear).…”

Section: Methodsmentioning

confidence: 99%

“…Both the Tpm1 protein (Tpm1p) and the less abundant Tpm2 protein (Tpm2p) have been shown to stabilize actin filaments that subsequently are bundled together to form actin cables (4). Although tpm2 mutations have little effect on gross actin cable structure in yeast cells, tpm1 mutants lack visible actin cables (5,11). Recent work established that yeast Tpm1p is also acetylated N-terminally, and that this acetylation is critical for normal binding and stabilization of filamentous actin (12).…”

mentioning

confidence: 99%

“…In nonmuscle cells, which lack troponin, its function is believed to consist primarily of filament stabilization (3,4). Tropomyosin exists in the cell as a parallel coiled-coil dimer that binds longitudinally to the actin filament and spans an integral number of actin monomers (four to seven, depending on cell type) (1,5). In addition, the protein interacts with itself in head-to-tail fashion, forming a spiraling polymer (6).…”

mentioning

confidence: 99%

“…The budding yeast Saccharomyces cerevisiae contains two tropomyosin genes, TPM1 and TPM2 (5,11). Both the Tpm1 protein (Tpm1p) and the less abundant Tpm2 protein (Tpm2p) have been shown to stabilize actin filaments that subsequently are bundled together to form actin cables (4).…”

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confidence: 99%

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Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin–actin interactions in budding yeast

Singer

Shaw

2003

Proc. Natl. Acad. Sci. U.S.A.

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The evolutionarily conserved Mdm20 protein (Mdm20p) plays an important role in tropomyosin-F-actin interactions that generate actin filaments and cables in budding yeast. However, Mdm20p is not a structural component of actin filaments or cables, and its exact function in cable stability has remained a mystery. Here, we show that cells lacking Mdm20p fail to N-terminally acetylate Tpm1p, an abundant form of tropomyosin that binds and stabilizes actin filaments and cables. The F-actin-binding activity of unacetylated Tpm1p is reduced severely relative to the acetylated form. These results are complemented by the recent report that Mdm20p copurifies with one of three acetyltransferases in yeast, the NatB complex. We present genetic evidence that Mdm20p functions cooperatively with Nat3p, the catalytic subunit of the NatB acetyltransferase. These combined results strongly suggest that Mdm20p-dependent, N-terminal acetylation of Tpm1p by the NatB complex is required for Tpm1p association with, and stabilization of, actin filaments and cables.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin–actin interactions in budding yeast

Singer

Shaw

2003

Proc. Natl. Acad. Sci. U.S.A.

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Review: An Overview of theSaccharomyces cerevisiae Microtubule and Microfilament Cytoskeleton

Winsor

Schiebel

1997

Yeast

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A potential role of the cytoskeleton ofSaccharomyces cerevisiae in a functional organization of glycolytic enzymes

Götz

Schlüter

Shoham

et al. 1999

Yeast

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Numerous individual enzymes participate in a given synthetic or degradative pathway in which the product of one reaction becomes the substrate for the subsequent enzyme. This raises the question of whether the product of one ‘soluble’ enzyme diffuses freely through the available cell volume, where it accidentally collides with the subsequent ‘soluble’ enzyme. Alternatively, enzymes acting in a given pathway may be organized in ordered structures, metabolons. Certain glycolytic enzymes have been shown to co‐localize with the cytoskeleton in mammalian cells. We deleted genes coding for proteins associated with the cytoskeleton of Saccharomyces cerevisiae: TPM1 coding for tropomyosin, SAC6 for fimbrin and CIN1 for a microtubule‐associated protein. Single deletions or deletions of two such genes had no effect on the specific activities of glycolytic enzymes, or on the rates of glucose consumption and ethanol production. However, the concentrations of glycolytic metabolites during a switch from a gluconeogenic mode of metabolism, growth on an ethanol medium, to glycolysis after glucose addition showed transient deviations from the normal change in metabolite concentrations, as observed in wild type cells. However, all metabolites in mutant strains reached wild‐type levels within 2–4 h after the shift. Only ATP levels remained low in all but the tmp1‐Δ–sac6‐Δ double mutant strains. These observations can be interpreted to mean that metabolic reorganization from a gluconeogenic to a glycolytic metabolism is facilitated by an intact cytoskeleton in yeast. Copyright © 1999 John Wiley & Sons, Ltd.

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Tropomyosin is essential in yeast, yet the TPM1 and TPM2 products perform distinct functions.

Abstract: Abstract. Sequence analysis of chromosome IX of Saccharomyces cerevisiae revealed an open reading frame of 166 residues, designated TPM2, having 64.5 % sequence identity to

Cited by 133 publications

References 42 publications

Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin–actin interactions in budding yeast

Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin–actin interactions in budding yeast

Review: An Overview of theSaccharomyces cerevisiae Microtubule and Microfilament Cytoskeleton

A potential role of the cytoskeleton ofSaccharomyces cerevisiae in a functional organization of glycolytic enzymes

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