Identification of the in vitro translation products of adenovirus mRNA by immunoprecipitation

Öberg, Bo; Saborío, José L.; Persson, Torgny; Everitt, Einar; Philipson, Lennart

doi:10.1128/jvi.15.1.199-207.1975

Cited by 61 publications

(29 citation statements)

References 30 publications

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“…is well established from studies on protein synthesis both in vivo (1) and in vitro (2,7,15). Therefore, we suggest that the complexes identified here are related to mature adenovirions in a precursor-product relationship.…”

supporting

confidence: 66%

Synthesis and processing of the precursor to the major core protein of adenovirus type 2

Everitt¹,

Meador²,

Levine³

1977

J Virol

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An isopycnic Metrizamide-detergent gradient system was developed in which the newly synthesized precursor (polypeptide P-VII) to the major core protein of adenovirus type 2 (polypeptide VII) was confined to a spectrum of complexes with densities equal to or higher than that of adenovirions. The majority of the newly synthesized P-VII was, at the beginning of the logarithmic period of virus production, present as an entity of protein density. This pool of P-VII was efficiently depleted. P-VII was also associated with high-molecular-weight structures of intermediate density, sharing some properties with empty capsids or incomplete particles. The transfer of P-VII from the intermediate-density region was not quantitative, and only particles of true virion density subsequently contained polypeptide VII. No structures equivalent to the core structure of disrupted virions or identical to incomplete particles were detected in this system. A temperature-dependent transition of radioactivity from polypeptide P-VII into polypeptide VII was also detectable after in vitro incubation of P-VIIcontaining complexes. Addition of Ad2-infected cell extracts was required for processing of complexes derived from regions of protein density, whereas P-VII was processed spontaneously upon incubation in complexes of virion density.

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supporting

confidence: 66%

Synthesis and processing of the precursor to the major core protein of adenovirus type 2

Everitt¹,

Meador²,

Levine³

1977

J Virol

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“…When the extracts were incubated with the wheat germ cocktail, 0.2 vol. of a solution used to supplement wheat germ extracts for in vitro translation (Oberg et al, 1975) was added to the brain extracts. This solution contained 120 mM-Hepes (N-2-hydroxyethyl piperazine-N'-2-ethanesulfonic acid), pH 7.6,0.36 M-KCI, 4.5 mM-DTT, 6 mM-ATP, 1.2 mM-GTP, 24 mg ofcreatine phosphate/ml, 240 pg of creatine phosphokinase/ml, and 144 p~ of each of the 20 amino acids used for in v i t r o translation.…”

Section: In Vitro Incubationsmentioning

confidence: 99%

“…These results imply that if Weactin is converted into Ply-actin as a result of posttranslational modifications, the in vitro translational system contains all that is required for the processing to take place. Based on those results, in the next experiment of this series aliquots of the crude brain extract labeled in vivo with [ 35S]methionine were incubated in vitro in the presence of the cocktail used for in vitro translation in the wheat germ system (Oberg et al, 1975). As shown in Fig.…”

Section: Gi€-actinmentioning

confidence: 99%

Posttranslational Processing of Brain Actin

Palmer

Vega

Grana

et al. 1980

Journal of Neurochemistry

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Two short‐lived isoforms of actin, named δ‐ and ε‐actin, have been detected in brain extracts from rats labeled in vivo with [35S]methionine. These two molecular species have PI values slightly more basic than β‐ and γ‐actin, the stable isoforms of the protein found in brain tissue. Under the appropriate incubation conditions δ‐ and ε‐actin, synthesized in vivo, can be converted in vitro into β‐ and γ‐actin. This posttranslational processing of δ‐ and ε‐actin requires acetyl coenzyme A, suggesting that an acetylation step, presumably of the NH2‐terminal end, is involved in the transformation of these proteins into β‐ and γ‐actin.

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“…In vitro translation in the cofactor-free system was studied under the following conditions. A wheat germ extract was prepared as described previously (Oberg et al, 1975), except that the extract was centrifuged at 100,000 x g for 90 rnin prior to chromatography on Sephadex G-25. The reaction mixtures contained 40%…”

Section: In Vitro Translation Of Rnamentioning

confidence: 99%

Brain Actin Synthesized In Vitro Undergoes Two Different and Sequential Posttranslational Modifications

Saborío

Palmer

1981

Journal of Neurochemistry

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The have studied the posttranslational processing of actin molecules synthesized in a cell-free system. The results of these experiments indicate that during the in vitro synthesis of the actins from rat brain the primary translational products undergo two different and sequential posttranslational modifications. These modifications are accompanied by slight changes in the isoelectric points of the proteins and can be detected by isoelectric focusing analysis. The same posttranslational modifications can be detected during the in vitro synthesis of chick embryo skeletal muscle actin. The evidence presented suggest that the first posttranslational modification may correspond to the methylation of a histidine residue, and the second modification most likely corresponds to the acetylation of the NH(2)-terminal amino acid residues of actin molecules.

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Identification of the in vitro translation products of adenovirus mRNA by immunoprecipitation

Cited by 61 publications

References 30 publications

Synthesis and processing of the precursor to the major core protein of adenovirus type 2

Synthesis and processing of the precursor to the major core protein of adenovirus type 2

Posttranslational Processing of Brain Actin

Brain Actin Synthesized In Vitro Undergoes Two Different and Sequential Posttranslational Modifications

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