Protein synthesis in yeast. II. Purification and properties of the elongation factor 1 from Saccharomyces cerevisiae.

The effect of Shiga toxin, from Shigella dysenteriae 1, on the component reactions of peptide elongation were investigated. Enzymic binding of [3H]phenylalanine-tRNA to reticulocyte ribosomes was inhibited by 50% at 7 nM toxin. Elongation factor 1 (eEF-1)-dependent GTPase activity was also inhibited. Both reactions were not restored by addition of excess eEF-1 protein. In contrast, toxin concentrations of 200 nM were required to inhibit by 50% the elongation factor 2 (eEF-2)-dependent translocation of aminoacyl-tRNA on ribosomes. Addition of excess eEF-2 restored translocation activity. The eEF-2-dependent GTPase activity was unaffected at toxin concentrations below 100 nM, and Shiga-toxin concentrations of up to 1,000 nM did not affect either GTP.eEF-2.ribosome complex-formation or peptidyltransferase activity. Thus Shiga toxin closely resembles alpha-sarcin in action, both being primary inhibitors of eEF-1-dependent reactions. In contrast, the 60 S ribosome inactivators ricin and phytolaccin are primary inhibitors of eEF-2-dependent reactions of peptide elongation.

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The effect of guanosine nucleotides on the multiple forms of protein synthesis elongation factor 1 from wheat embryos

Archives of Biochemistry and Biophysics ◽

10.1016/0003-9861(73)90461-x ◽

1973 ◽

Vol 159 (1) ◽

pp. 353-361 ◽

Cited By ~ 31

Author(s):

Adela Tarragó ◽

Jorge E. Allende ◽

Betty Redfield ◽

Herbert Weissbach

Keyword(s):

Protein Synthesis ◽

Elongation Factor ◽

Multiple Forms ◽

Wheat Embryos ◽

Elongation Factor 1

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Increased expression of Saccharomyces cerevisiae translation elongation factor 1 alpha bypasses the lethality of a TEF5 null allele encoding elongation factor 1 beta.

Genetics ◽

10.1093/genetics/141.2.481 ◽

1995 ◽

Vol 141 (2) ◽

pp. 481-489 ◽

Cited By ~ 8

Author(s):

T G Kinzy ◽

J L Woolford

Keyword(s):

Saccharomyces Cerevisiae ◽

Null Allele ◽

Elongation Factor ◽

Wild Type ◽

Translation Elongation Factor ◽

Gene Encoding ◽

Translation Elongation ◽

Dominant Mutant ◽

Cold Sensitive ◽

Elongation Factor 1

Abstract Translation elongation factor 1beta (EF-1beta) catalyzes the exchange of bound GDP for GTP on EF-1alpha. The lethality of a null allele of the TEF5 gene encoding EF-1beta in Saccharomyces cerevisiae was suppressed by extra copies of the TEF2 gene encoding EF-1alpha. The strains with tef5::TRP1 suppressed by extra copies of TEF were slow growing, cold sensitive, hypersensitive to inhibitors of translation elongation and showed increased phenotypic suppression of +1 frameshift and UAG nonsense mutations. Nine dominant mutant alleles of TEF2 that cause increased suppression of frameshift mutations also suppressed the lethality of tef5::TRP1. Most of the strains in which tef5::TRP1 is suppressed by dominant mutant alleles of TEF2 grew more slowly and were more antibiotic sensitive than strains with tef5::TRP1 is suppressed by wild-type TEF2. Two alleles, TEF2-4 and TEF2-10, interact with tef5::TRP1 to produce strains that showed doubling times similar to tef5::TRP1 strains containing extra copies of wild-type TEF2. These strains were less cold sensitive, drug sensitive and correspondingly less efficient suppressor of +1 frameshift mutations. These phenotypes indicate that translation and cell growth are highly sensitive to changes in EF-1alpha and EF-1beta activity.

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