In vitro phosphorylation of histones H5, H2A, H2B and of the dimer H2A‐H2B by a cyclic AMP‐dependent protein kinase from rat pancreas

Martinage, Arlette; Mangeat, Paul; Lainé, Bernard; Couppez, Maurice; Sáutière, Pierre; Marchis-Mouren, G.; Biserte, G

doi:10.1016/0014-5793(80)80249-3

Cited by 15 publications

(13 citation statements)

References 25 publications

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“…The phosphorylation sites of histone H5 phosphorylated with the cAMP-dependent protein kinase from rat pancreas [8] are given by comparison.…”

Section: Resultsmentioning

confidence: 99%

“…As observed in histone H5 phosphorylated with a cAMP-dependent kinase from rat pancreas [8], the serine residues phosphorylated with the HI-specific cAMP-independent kinase are all located within regions in predicted 13-turn conformation except Ser3 [ 14,15]. In fact, the specificity of a given protein kinase is basically related to the recognition of specific amino acid sequences.…”

Section: Resultsmentioning

confidence: 99%

“…Tryptic hydrolysis, fractionation of tryptic hydrolysate and identification of phosphorylated sites were performed as in [8]. Table 1 Sites of in vitro phosphorylation of histone H5 determined from 3~P-labelled tryptic peptides sites are located in a sequence B-X-Ser where B is a basic amino acid and X any amino acid…”

Section: Localization Of Phosphorylation Sitesmentioning

confidence: 99%

“…Sites of phosphorylation of histone H5 have been investigated in vivo [4], and in vitro using the catalytic subunit of cyclic AMPdependent protein kinase from pig brain [7] and from rat pancreas [8]. Even if the specificity is different from one kinase to another, the sites of phosphorylation in histone H5 are distributed in vitro as in vivo in two distinct regions of the protein: the amino-terminal region (residues 1-21) and the carboxy-terminal region (residues 101-189); in all cases, no site has been detected in the globular part of the molecule (residues 22-100) [9].…”

Section: Introductionmentioning

confidence: 99%

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Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

et al. 1981

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“…The phosphorylation sites of histone H5 phosphorylated with the cAMP-dependent protein kinase from rat pancreas [8] are given by comparison.…”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Localization Of Phosphorylation Sitesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

et al. 1981

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“…Individual histones and the (H3-H4)2 complexes were phosphorylated by a cAMP-dependent protein kinase isolated from rat pancreas as in [12] but at 0.2-0.3/2g enzyme/ml in the presence of 0.4 mM [7-32P] ATP (10 Ci/mmol) prepared as in [ 17].…”

Section: Methodsmentioning

confidence: 99%

Study of in vitro phosphorylation of histones H3, H4 and of the non‐acetylated and acetylated tetramers (H3–H4)₂

et al. 1981

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Nuclear import of protein kinases and cyclins

Boulikas

1996

J. Cell. Biochem.

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Karyophilic and acidic clusters were found in most nonmembrane serine/threonine protein kinases whose primary structure was examined. These karyophilic clusters might mediate the anchoring of the kinase molecules to transporter proteins for their regulated nuclear import and might constitute the nuclear localization signals (NLS) of the kinase molecules. In contrast to protein transcription factors that are exclusively nuclear possessing strong karyophilic peptides composed of at least four arginines (R) and lysines (K) within an hexapeptide flanked by proline and glycine helix-breakers, protein kinases often contain one histidine and three K+R residues; this is proposed to specify a weak NLS structure resulting in the nuclear import of a fraction of the total cytoplasmic kinase molecules as well as in their weak retention in the different ionic strength nuclear environment. Putative NLS peptides in protein kinases may also contain hydrophobic or bulky aromatic amino acids proposed to further diminish their capacity to act as strong NLS. Most kinases lacking karyophilic clusters (c-Mos, v-Mos, sea star MAP, and yeast KIN28, SRA1, SRA3, TPK1, TPK2) also lack acidic clusters, which is in contrast to most kinases containing both acidic and karyophilic peptides; this and the presence of R/K clusters in the transporter proteins supports a role of acidic clusters on kinases in nuclear import. Cyclins B lack karyophilic signals and are proposed to be imported into nuclei via their association with Cdc2.

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In vitro phosphorylation of histones H5, H2A, H2B and of the dimer H2A‐H2B by a cyclic AMP‐dependent protein kinase from rat pancreas

Cited by 15 publications

References 25 publications

Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

Study of in vitro phosphorylation of histones H3, H4 and of the non‐acetylated and acetylated tetramers (H3–H4)₂

Nuclear import of protein kinases and cyclins

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In vitro phosphorylation of histones H5, H2A, H2B and of the dimer H2A‐H2B by a cyclic AMP‐dependent protein kinase from rat pancreas

Cited by 15 publications

References 25 publications

Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

Phosphorylated sites of chicken erythrocyte histone H5 by a cyclic AMP‐independent protein kinase from mouse plasmocytoma cells

Study of in vitro phosphorylation of histones H3, H4 and of the non‐acetylated and acetylated tetramers (H3–H4)2

Nuclear import of protein kinases and cyclins

Contact Info

Product

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Study of in vitro phosphorylation of histones H3, H4 and of the non‐acetylated and acetylated tetramers (H3–H4)₂