Eukaryotic Protein Synthesis

Moldave, Kivie

doi:10.1146/annurev.bi.54.070185.005333

Cited by 529 publications

(219 citation statements)

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“…The rate of protein synthesis appears to decline with age in many animal species (Lints & Bourgois, 1985;Moldave, 1985;Levenbook, 1986;Webster, 1986 -but see Finch, 1990). Experiments performed by Webster (1985) suggested that the age-related decline in protein synthesis in Drosophila might result from the decreased transcription of the EF-1o gene.…”

Section: Introductionmentioning

confidence: 99%

P-element inserts in transgenic flies: a cautionary tale

Kaiser¹,

GASSER²,

ACKERMANN³

et al. 1997

Heredity

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The fruitfly, Drosophila melanogaster, can be transfected with P-elements and induced to overexpress a transfected gene whose impact on lifespan can be measured. Here, it is reported that in previous experiments a transfected gene was not expressed. This suggested a new statistical analysis indicating that (1) the size of the insert, the position and the interactions of the insert with the genetic backgrounds into which the P-element are inserted have effects on lifespan similar to those attributed to overexpression; (2) these effects occur without expression of the transfected gene; and (3) effects of interactions with backgrounds and effects of positions are as large as responses to six generations of strong directional artificial selection. Reports of effects of overexpression of transfected genes on lifespan in Drosophila melanogaster may be experimental artefacts. Credible experiments on the phenotypic effects of transgenesis need proper controls for the effects of insert size and position and should estimate the magnitudes of interactions of treatment with genetic backgrounds.

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Section: Introductionmentioning

confidence: 99%

P-element inserts in transgenic flies: a cautionary tale

Kaiser¹,

GASSER²,

ACKERMANN³

et al. 1997

Heredity

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“…The translation in yeasts and fungi requires three kinds of elongation factors; EF-1, EF-2 and EF-3 (1)(2)(3)(4)(5). EF-3 is specific to yeasts and fungi, while EF-1 and EF-2 are common to all organisms (in prokaryotes, the counterparts of EF-1 and EF-2 are referred to as EFT and EF-G, respectively).…”

Section: Introductionmentioning

confidence: 99%

A monoclonal antibody specific for carboxy‐terminal region of yeast translation elongation factor‐3 inhibits ribosome‐activated ATPase activity but not intrinsic ATPase activity

et al. 1996

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Summary Elongation factor-3 (EF-3) is an essential translation elongation factor specific to yeasts and fungi. When EF-3 interacts with yeast ribosomes, its ATPase activity, which is indispensable for the function of EF-3 in translation, is drastically enhanced. In this study, a monoclonal antibody specific for the carboxy-terminal region inhibited the ribosome-activated ATPase activity of EF-3, while it did not inhibit the intrinsic ATPase activity of EF-3. The results suggest that the carboxy-terminal region of EF-3 is involved in the interaction with yeast ribosomes. The monoclonal antibody also inhibited poly(U)-directed poly(Phe) synthesis, which indicates that the carboxy-terminal region is important for EF-3 to express its function in the polypeptide elongation cycle.

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“…The heavy form ranges in Mr from 140 000 to 800 000 [1,2]. A significant portion of EF-1 is tightly complexed with valyl-tRNA synthetase [3,4].…”

Section: Introductionmentioning

confidence: 99%

Comparison of phosphorylation of elongation factor 1 from different species by caScin kinase II

1990

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One subunit of EF-I or EF-Ifl7 from Artemia salina, wheat germ and rabbit reticulocytes is modified by casein kinase II. The subunit corresponds to the low Mr subunit of EF-1 (26000-36000) which functions along with a higher Mr subunit (46000~8000), to catalyze the exchange of GDP for GTP on EF-lct. The factor from Artemia and wheat germ is phosphorylated directly on serine by casein kinase II whereas a modulatory compound is required for phosphorylation of EF-1 from reticulocytes. Polylysine increases the rate of phosphorylation of EF-1 from reticulocytes by 24-fold; both serine and threonine are modified. This suggests that polylysine may be substituting for a physiological regulatory compound which modulates phosphoryation in vivo.

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Eukaryotic Protein Synthesis

Cited by 529 publications

References 0 publications

P-element inserts in transgenic flies: a cautionary tale

P-element inserts in transgenic flies: a cautionary tale

A monoclonal antibody specific for carboxy‐terminal region of yeast translation elongation factor‐3 inhibits ribosome‐activated ATPase activity but not intrinsic ATPase activity

Comparison of phosphorylation of elongation factor 1 from different species by caScin kinase II

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