Reprocessing of Spent Nuclear Fuels

Walton, Gabriel; Merz, E.

doi:10.1007/978-3-662-06014-8_2

Cited by 2 publications

(3 citation statements)

References 324 publications

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“…The RII regulatory subunit of the cAMP-dependent kinase was phosphorylated in vitro by casein II kinase at the same site as in vivo (Carmichael et al, 1982;Hemmings et al, 1982). Similarly, the site phorphorylated on HMG protein 14 by casein II kinase in vitro was the same site phosphorylated in vivo suggesting that endogenous casein II kinase catalyzed the reaction in vivo (Walton and Gill, 1983;Walton et al, 1985).…”

Section: Discussionmentioning

confidence: 96%

“…TIME(min) A number of proteins have been shown to serve as in vitro substrates for casein II kinases. These include glycogen synthase (Meggio et al, 1981), translation initiation factors (Hathaway et al, 1979), RNA polymerase I and II (Dahmus, 1981;Duceman et al, 1981;Stetler and Rose, 1982), troponin-T (Villar-Palasi and Kumon, 1981), high mobility group (HMG) protein 14 (Walton and Gill, 1983;Walton et al, 1985), the regulatory subunit RuI of the cAMP-dependent protein kinase (Carmichael et al, 1982;Hemmings et al, 1982) and topoisomerase II (Ackerman et al, 1985). Phosphorylation of Drosophila topoisomerase II by homologous casein II kinase (Ackerman et al, 1985) resembled the phosphorylation characteristics of topoisomerase I in that phosphorylation had a stimulatory effect on enzymatic activity, serine was the phosphate-acceptor amino acid and the kinase had a high affinity for the topoisomerase (Durban et al, 1983;Mills et al, 1982).…”

Section: Discussionmentioning

confidence: 99%

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Topoisomerase I phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells.

Durban¹,

Goodenough²,

Mills³

et al. 1985

The EMBO Journal

107

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Changes in phosphorylation modulate the activity of topoisomerase I in vitro. Specifically, enzymatic activity is stimulated by phosphorylation with a purified protein kinase (casein kinase type II). The purpose of this study was to compare the sites that are phosphorylated in vitro by casein kinase type II with the site(s) phosphorylated in vivo in rapidly growing Novikoff hepatoma cells. Topoisomerase I labeled in vitro was characterized by three major tryptic phosphopeptides (I‐III). Separation of these peptides by a C18‐reverse phase h.p.l.c. column resulted in their elution at fractions 18 (I), 27 (II) and 44 (III) with 17%, 22.5% and 33% acetonitrile, respectively. In contrast, only one major phosphopeptide was identified by h.p.l.c. in topoisomerase I labeled in vivo. This phosphopeptide eluted at fraction 18 corresponding to the elution properties of phosphopeptide I labeled in vitro. It also co‐migrated with tryptic phosphopeptide I when subjected to high‐voltage electrophoresis on thin‐layer cellulose plates. Preliminary experiments suggest that phosphorylation occurs at a serine residue six amino acids from the N‐terminus of the peptide. These data indicate that topoisomerase I is phosphorylated in vivo and in vitro within the same tryptic peptide and suggest that topoisomerase I is phosphorylated in vivo by casein kinase II.

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Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Topoisomerase I phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells.

Durban¹,

Goodenough²,

Mills³

et al. 1985

The EMBO Journal

107

View full text Add to dashboard Cite

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“…In bovine thyroid slices, serine 6 is phosphorylated in response to thyrotrophin (Walton et al, 1984). In HeLa cells, serine 89, which is phosphorylated during G2/M, may be phosphorylated in vitro by casein kinase II (Walton and Gill, 1983;Walton et al, 1985). Further, an endogenous metaphase-specific HMG-14 kinase associated with isolated HeLa chromosomes has been reported (Paulson and Taylor, 1982).…”

Section: Discussionmentioning

confidence: 99%

A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.

et al. 1994

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The rapid, transient induction of 80‐100 immediate‐early (IE) genes upon mitogenic stimulation occurs irrespective of protein synthesis and is mediated by modification of existing proteins. Two mechanisms, not mutually exclusive, involving modification either of sequence‐specific transcription factors or of structural chromatin proteins primed by pre‐association with responsive effectors are conceivable. Here, we show that upon IE gene induction, the non‐histone high‐mobility‐group protein HMG‐14, but not the related protein HMG‐17, becomes serine phosphorylated in its basic, amino‐terminal region close to where it binds nucleosomal DNA. Phosphorylation, normally transient, occurs independent of transcription and is quantitative and prolonged during superinduction. Brief micrococcal nuclease digestion substantially releases HMG‐14 from nuclei in the mononucleosome‐bound state. Finally, mononucleosomes prepared from mitogen‐stimulated, but not control, cells contain a mitogen‐activated kinase that phosphorylates HMG‐14 in vitro on the same site(s) as in intact cells. The association of HMG‐14 and its mitogen‐activated kinase with nuclease‐sensitive mononucleosomes has implications for models of mitogen‐stimulated IE gene induction.

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Reprocessing of Spent Nuclear Fuels

Cited by 2 publications

References 324 publications

Topoisomerase I phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells.

Topoisomerase I phosphorylation in vitro and in rapidly growing Novikoff hepatoma cells.

A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.

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