Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 7

1.
FIG. 2

FIG. 2. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Conserved cluster of residues in S. cerevisiae, S. pombe (fission yeast), X. laevis, B. mori (silkworm), Oryza sativa (rice), A. salina, wheat germ, T. cruzi, rabbit, and human EF-1β proteins and hEF-1δ. Hyphens indicate residues identical to S. cerevisiae EF-1β.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
2.
FIG. 7

FIG. 7. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Total methionine incorporation in strains containing wild-type TEF5 (TKY235, circles), the tef5-1 allele (TKY238, squares) (A), or the tef5-7 allele (TKY243, triangles) (B). Strains were grown to mid-log phase in C-Met and labeled for varying times in [35S]methionine. Incorporation (in counts per minute) is expressed per A600 unit of cells.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
3.
FIG. 6

FIG. 6. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Suppression of the Cs defects of mutant strains containing tef5-1 (TKY238 S121L) (A) and tef5-4 (TKY236 K120R S121L) (B) by excess yEF-1α. Plasmids bearing the URA3 marker and no TEF gene (pRS316), TEF2 CEN, TEF2 2μm, TEF3 CEN, and TEF4 CEN were transformed into the strain and grown in C-Ura. Equal numbers of cells for each strain were spotted in 1/10 serial dilutions and grown on C-Ura at 30 and 13°C.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
4.
FIG. 5

FIG. 5. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Excess copies of the gene encoding yEF-1α but not of that encoding yEF-1γ (TEF3 and TEF4, respectively) result in a conditional growth defect in a wild-type strain. Strain TKY235 (TEF5 LEU2) was transformed with URA3 plasmids containing no TEF gene (pRS316), TEF2 CEN, TEF2 2μm, TEF3 CEN, and TEF4 CEN. The strains were grown at 30°C in liquid C-Ura, and equal numbers of cells for each were spotted in 1/10 serial dilutions and grown on C-Ura at 13, 24, 30, and 37°C.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
5.
FIG. 4

FIG. 4. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Growth defects of strains containing the tef5 mutant alleles. (A) Strains containing the lys2-801 allele (UAG) and either the wild-type TEF5 gene or one of the tef5-1 to tef5-10 alleles on a LEU2 CEN plasmid were grown at 30°C, and equal numbers of cells were spotted on YEPD medium. From top left are shown TKY235 (TEF5), TKY238 (tef5-1), TKY240 (tef5-2), TKY244 (tef5-3), TKY236 (tef5-4), TKY242 (tef5-5), TKY251 (tef5-6), TKY243 (tef5-7), TKY239 (tef5-8), TKY241 (tef5-9), and TKY237 (tef5-10). Growth was monitored following 3 to 7 days at 37, 30, 24, or 13°C. (B) Growth was monitored on complete medium–0.5 mg of paromomycin per ml (top) and C-Lys–0.5 mg of paromomycin per ml (bottom) for strains (from top left) TKY235 (TEF5), TKY238 (tef5-1), TKY240 (tef5-2), TKY244 (tef5-3), and TKY243 (tef5-7) following 7 days at 30°C.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
6.
FIG. 1

FIG. 1. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

Only the C terminus of EF-1β is essential in vivo. (A) Sequence of S. cerevisiae EF-1β indicating sites of truncations (underlined). (B) Western blot analysis of extracts of strains expressing the HA epitope-tagged full-length and truncated yEF-1β. Lanes from left to right are TKY285 (yEF-1β-HA), JWY4298 (yEF-1βΔ60-HA), JWY4299 (yEF-1βΔ85-HA), and TKY257 (yEF-1βΔ96-HA) grown in galactose and expressed from the GAL1 promoter. (C) Growth of strains expressing full-length and truncated yEF-1β. Strains from the top are TKY285 (yEF-1β-HA), JWY4298 (yEF-1βΔ60-HA), JWY4299 (yEF-1βΔ85-HA), and TKY257 (yEF-1βΔ96-HA) grown on YEP-galactose at 30°C for 4 days. (D) Comparison of expression from the GAL1 and TEF5 promoters. Lanes from left to right are TKY285 (GAL1 promoter, yEF-1β-HA) and the TEF5 promoter expressing full-length yEF-1β-HA (TKY258) and truncated yEF-1βΔ96-HA (TKY266). (E) Growth of strains expressing (from top to bottom) TKY285 (GAL1 promoter, yEF-1β-HA) and TEF5 promoter expressing full-length yEF-1β-HA (TKY258) and truncated yEF-1βΔ96-HA (TKY266) grown on YEP-galactose at 30°C for 4 days. All blots were probed with anti-HA and anti-phosphatidylglycerol kinase antibodies. For panels B and D, MW indicates molecular mass in kilodaltons.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.
7.
FIG. 3

FIG. 3. From: Mutations in Elongation Factor 1?, a Guanine Nucleotide Exchange Factor, Enhance Translational Fidelity.

The human homolog of yEF-1β, but not the hEF-1β-like protein EF-1δ, is functional in yeast. The cDNAs encoding hEF-1β and hEF-1δ were fused to the HA epitope tag and expressed under the control of the yeast GAL1 promoter. (A) Western blot analysis indicates that HA-tagged full-length forms of hEF-1β and hEF-1δ are expressed under the GAL1 promoter. Lanes from left to right are hEF-1δ-HA (JWY4229 with pTKB301), hEF-1β-HA (TKY256), yEF-1β-HA (TKY169), and a strain containing an untagged form of yEF-1β (JWY4229). (B) Truncated hEF-1δ is stably expressed under the control of the GAL1 promoter in yeast. Lanes from left to right are hEF-1δΔ172-HA (JWY4229 with pTKB158) and yEF-1βΔ96-HA (TKY257). (C) Growth of strains containing HA-tagged full-length forms of yEF-1β-HA (TKY169, top) and hEF-1β-HA (TKY256, bottom) on C-Ura-galactose at 30°C for 4 days. (D) Growth of strain JWY4229 expressing full-length and truncated hEF-1δ. The strain contains the chomosomal wild-type TEF5 gene and (from top to bottom) pRS316 (empty vector), hEF-1δ-HA, or hEF-1δΔ172-HA and was grown on C-Ura-galactose at 30°C for 4 days. (E) yEF-1β, hEF-1β, and hEF-1δ coimmunoprecipitate with yEF-1α. Shown are Western blots with anti-HA antibodies of a portion of the supernatants (S) and the entire pellets (P) of an immunoprecipitation of yeast extracts containing yEF-1β-HA (TKY169), hEF-1β-HA (TKY286), and hEF-1δ-HA (TKY4231 plus pTKB151) precipitated with an anti-yEF-1α polyclonal antibody. For panels A, B, and E, MW indicates molecular mass in kilodaltons.

Anne Carr-Schmid, et al. Mol Cell Biol. 1999 August;19(8):5257-5266.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk