Association of a GDP binding activity with initiation factor eIF-2 from calf liver

Stringer, Evan A.; Chaudhuri, Asok; Maitra, Umadas

doi:10.1016/0006-291x(77)90764-1

Cited by 14 publications

(2 citation statements)

References 12 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gill (1975, 1976) have proposed that mRNA translation in reticulocytes may be regulated by GTP to GDP ratios which are dependent upon the energy state of the cell. GDP strongly inhibits ter-nary complex formation between eF-2, GTP, and met-tRNAf Gill, 1975, 1976;Stringer et al, 1977). However, in reticulocyte lysates, elongation is more sensitive to guanylate charge than initiation is (Safer and Jagus, 1979).…”

Section: Discussionmentioning

confidence: 99%

Coordinate regulation of polypeptide chain initiation and elongation in rabbit reticulocytes

Binninger

Weber

1984

Journal Cellular Physiology

View full text Add to dashboard Cite

Under normal conditions, reticulocytes synthesize alpha- and beta-globin polypeptides at equal rates. Incubation in the absence of hemin or under anoxia or hypertonic stress (100 mM excess NaCl) reduces the rate of protein synthesis to 30-50% of control levels. However, only hemin deprivation causes a reduction in polyribosome size and preferential inhibition of alpha-globin synthesis consistent with specific reduction in the rate of polypeptide chain initiation. Polyribosomal profiles are unaffected by anoxic or hypertonic stress and the ratio of alpha:beta globin synthesis remains close to unity. Measurement of ribosome transit time indicates that anoxic or hypertonic stress causes a decrease in the rate of polypeptide chain elongation that varies with the degree of inhibition of protein synthesis. Ribosomes isolated from stressed cells exhibit a reduced ability to bind 35S-met-tRNAf, suggesting that the ability to form initiation complexes is also impaired. These results suggest that reticulocytes, unlike nucleated cell lines, can coordinately reduce rates of initiation and elongation in response to certain physiological stresses.

show abstract

Section: Discussionmentioning

confidence: 99%

Coordinate regulation of polypeptide chain initiation and elongation in rabbit reticulocytes

Binninger

Weber

1984

Journal Cellular Physiology

View full text Add to dashboard Cite

show abstract

“…Similar results have been reported for initiation factor from other sources; however, the magnitude of inhibition varies considerably. Stringer et al (1977) show approximately an 85% inhibition of ternary complex formation for their purified liver factor when the concentration of GDP is one-tenth that of GTP. When GDP is present in equimolar concentration with GTP, ternary complex formation is inhibited 32% with a purified preparation of initiation factor from A .…”

Section: Discussionmentioning

confidence: 99%

Regulation of the First Step of the Initiation of Brain Protein Synthesis by Guanosine Diphosphate

Dwyer

Wasterlain

1980

Journal of Neurochemistry

View full text Add to dashboard Cite

Initiation factor elF-2-like activity has been measured in the 0.5 M-KCI wash of rat brain microsomes. Ternary complex formation (eIF-2 . GTP . Met-tRNA,), one of the early steps in protein synthesis initiation, is optimal in a high-[K+], low-"a+] environment. Mgz+, Ca2+, Li+, spermine, and spermidine reduce, and the antibiotic aurin tricarboxylic acid can effectively eliminate ternary complex formation. The formation of ternary complex requires GTP or its nonhydrolyzable analog, GMP-P(NH)P. Ternary complex formation is particularly sensitive to the ratio of GDP to GTP. When the ratio of GDP to GTP added is l:lO, ternary complex formation is inhibited between 40 and 50% over a 30-fold concentration range of GTP. Other nucleotides exert little inhibition. These results suggest that the regulation of brain protein synthesis initiation may be tightly linked to the ratios of guanosine nucleotide c o n c e n t r a t i o n s in b r a i n t i s s u e . K e y words: Protein-Guanosine diphosphate-Regulation-Brain-Initiation.

show abstract

Function of eukaryotic ribosomes

Bielka¹

1982

The Eukaryotic Ribosome

View full text Add to dashboard Cite

Association of a GDP binding activity with initiation factor eIF-2 from calf liver

Cited by 14 publications

References 12 publications

Coordinate regulation of polypeptide chain initiation and elongation in rabbit reticulocytes

Coordinate regulation of polypeptide chain initiation and elongation in rabbit reticulocytes

Regulation of the First Step of the Initiation of Brain Protein Synthesis by Guanosine Diphosphate

Function of eukaryotic ribosomes

Contact Info

Product

Resources

About