Evidence for an inhibitor of protein synthesis in rabbit reticulocytes activated by high pressure

Henderson, A. B.; Hardesty, Boyd

doi:10.1016/0006-291x(78)91048-3

Cited by 26 publications

(3 citation statements)

References 19 publications

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“…These low salt/Mg 2ϩ -induced transitions, however, are reversed simply by incubating the ribosomes at standard Mg 2ϩ and salt concentrations at moderate temperatures, whereas the conversion of 80S to 80S* complexes does not occur in the absence of the HSW factors. A decrease in the activity of rabbit reticulocyte translation systems, apparently as the result of the pressure during ultracentrifugation, has also been reported (Henderson and Hardesty, 1978;Morley and Hershey, 1990). This inhibition was shown to result in part from activation of the hemin-controlled repressor (HCR), which is an eIF2 kinase (Henderson and Hardesty, 1978;Clemens, 1996).…”

Section: A New Step In Eukaryotic Translation Initiation?mentioning

confidence: 90%

“…A decrease in the activity of rabbit reticulocyte translation systems, apparently as the result of the pressure during ultracentrifugation, has also been reported (Henderson and Hardesty, 1978;Morley and Hershey, 1990). This inhibition was shown to result in part from activation of the hemin-controlled repressor (HCR), which is an eIF2 kinase (Henderson and Hardesty, 1978;Clemens, 1996). However, HCR is unlikely to be responsible for formation of low activity 80S complexes because HCR inhibits formation of the ternary complex, a step prior to 80S complex formation (see Figures 1 and 7).…”

Section: A New Step In Eukaryotic Translation Initiation?mentioning

confidence: 90%

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Kinetic dissection of fundamental processes of eukaryotic translation initiation in vitro

Lorsch

Herschlag

1999

The EMBO Journal

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Approaches have been developed for the kinetic dissection of eukaryotic translation initiation in vitro using rabbit reticulocyte ribosomes and a crude preparation of initiation factors. These new approaches have allowed the kinetics of formation of the 43S and 80S ribosomal complexes to be followed and have substantially improved the ability to follow formation of the first peptide bond. The results suggest the existence of a new step on the initiation pathway that appears to require at least one additional factor and the hydrolysis of GTP and may prepare the 80S complex for the formation of the first peptide bond. The initial kinetic framework and methods developed herein will allow the properties of individual species along the initiation pathway to be probed further and will facilitate dissection of the mechanistic roles of individual translation factors and their interplay with RNA structural elements.

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Section: A New Step In Eukaryotic Translation Initiation?mentioning

confidence: 90%

Section: A New Step In Eukaryotic Translation Initiation?mentioning

confidence: 90%

Kinetic dissection of fundamental processes of eukaryotic translation initiation in vitro

Lorsch

Herschlag

1999

The EMBO Journal

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“…Also, we do not believe that NAI could be a phosphatase inhibitor as it produces its effect in both crude and purified preparations of eIF-2a kinase, the latter of which lacks any protein phosphatase activity (not shown). A thermolabile inhibitor, HL, with an M, of about 40,000, has been found after subjecting the postribosomal supernatant from rabbit reticulocytes to high pressure (Henderson and Hardesty, 1978); further purification of NAI is necessary to determine whether it is the same inhibitor.…”

Section: Discussionmentioning

confidence: 99%

Partial Purification of a Novel N‐Ethylmaleimide‐Activated Translational Inhibitor from Adult Rat Brain

Alcázar

Garcı́a

et al. 1991

Journal of Neurochemistry

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A translational inhibitor that is activated by N-ethylmaleimide treatment can be found in the postmicrosomal fraction prepared from the brain of adult rats, but it is almost undetectable in the same fraction prepared from suckling animals. The inhibitor is thermolabile and remains in the supernatant fraction after precipitation at pH 5. During the purification procedure, the inhibitor in its unactivated state binds to the anion exchanger (diethylaminoethyl-cellulose) but not to the cation exchanger (phosphocellulose). Treatment with N-ethylmaleimide increases inhibitor affinity for the cation exchanger, and this chromatographic step purifies the inhibitor by 143-fold. Both the thermolabile nature and the behavior of the inhibitory activity during the different steps of the purification procedure suggest that this activity is most probably due to a protein. Although the addition of initiation factor 2 reverses the inhibition of protein synthesis in the presence of ATP and Mg2+, the inhibitor does not phosphorylate any of the initiation factor subunits "in vitro," which indicates that it does not contain any intrinsic protein kinase activity. However, its presence in both a crude and a purified preparation of a kinase of the alpha subunit of a brain eukaryotic initiation factor increases the phosphorylation of the alpha subunit of the initiation factor. The mechanism of action of this inhibitor is discussed.

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The Cytoplasmic Control of Protein Synthesis

Jackson

1982

Protein Biosynthesis in Eukaryotes

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Evidence for an inhibitor of protein synthesis in rabbit reticulocytes activated by high pressure

Cited by 26 publications

References 19 publications

Kinetic dissection of fundamental processes of eukaryotic translation initiation in vitro

Kinetic dissection of fundamental processes of eukaryotic translation initiation in vitro

Partial Purification of a Novel N‐Ethylmaleimide‐Activated Translational Inhibitor from Adult Rat Brain

The Cytoplasmic Control of Protein Synthesis

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