Protein-bound phosphorylserine in different tissues and organisms

Forsberg, Håkan; Zetterqvist, Örjan; Engström, Lorentz

doi:10.1016/0005-2795(69)90238-4

Cited by 23 publications

(4 citation statements)

References 5 publications

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“…Unlabeled methionine was substituted for [3H]Met, and [32P]orthophosphate was added followed by incubation for 10 h. In this time, the cells incorporated 5.9 nmol of phosphoryl groups/mg of protein. This number is consistent with that obtained previously by Forsberg et al (1969) of 6-10 nmol/mg of protein.…”

Section: Comparison Of the Levels Of Methyl Esterification Andsupporting

confidence: 93%

Methyl-esterified proteins in a mammalian cell line

Chelsky¹,

Ruskin²,

Koshland³

1985

Biochemistry

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Methyl esterification of carboxylic acid residues in intact mouse S49 lymphoma cells was examined, and at least 24 proteins were found to be modified. Cell fractionation revealed that a distinct set of these proteins could be found in each of the four fractions. Nuclei contained 11 methyl-esterified proteins at 12, 15.5, 18, 19, 39, 41, 45, 70, 90, 105, and 130 kilodaltons (kDa). Five proteins copurified with the plasma membrane/mitochondrial fraction at 13, 24, 25, 27, and 28 kDa. Two proteins at 32 and 56 kDa were in the microsomal fraction, and six were soluble at 16.5, 21, 24, 26, 34, and 36 kDa. Eleven of these proteins were [3H]methyl esterified when cell homogenates were incubated with S-adenosyl-L-[methyl-3H]methionine. The steady-state level of methyl group incorporation into protein in intact cells was approximately 118 pmol/mg of protein. Assuming the average protein is 40 kDa, there appears to be 1 methyl group per 210 proteins. This was compared to phosphorylation which gave approximately one phosphoryl group for every four proteins. Exogenously added L-[methyl-3H]methionine equilibrated with the cellular S-adenosylmethionine pool within 30 min which was sufficiently rapid to allow the rate of methyl group turnover to be determined. Most methyl-esterified proteins demethylated in a pulse--chase experiment with half-lives ranging from 2.6 to 9.3 h. When protein syn thesis was blocked with puromycin, amino acid backbone incorporation of methionine was reduced to 2% of control. Methyl group incorporation, however, was 39% of the control.(ABSTRACT TRUNCATED AT 250 WORDS)

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Section: Comparison Of the Levels Of Methyl Esterification Andsupporting

confidence: 93%

Methyl-esterified proteins in a mammalian cell line

Chelsky¹,

Ruskin²,

Koshland³

1985

Biochemistry

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“…Samples were analyzed after acid hydrolysis (2 M HCl, 100 "C, 20 h) by chromatography on Dowex 50 and Dowex 1 as previously described [30].…”

Section: Isolation Of Phosphorylated Amino Acidsmentioning

confidence: 99%

“…In order to verify that the phosphate label in the 72 000-M, polypeptide resides covalently linked to the protein moiety, the 32P-labeled polypeptide was hydrolyzed in 2 M HCI together with cold phosphorylserine and phosphorylthreonine. The hydrolysate was analyzed as previously described [30]. After correction for hydrolysis around 90% of the 32P label was recovered in phosphorylserine and around 10 % in phosphorylthreonine, clearly establishing that the DNA-binding protein is phosphorylated.…”

Section: Phosphorylation Of the Dna-binding Proteinmentioning

confidence: 99%

Purification and Characterization of the Phosphorylated DNA-Binding Protein from Adenovirus-Type-2-Infected Cells

Linné¹,

Jörnvall

Philipson³

1977

Eur J Biochem

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The virus‐coded 72000‐Mr DNA‐binding protein from adenovirus‐type‐2‐infected cells has been purified to homogeneity by DEAE‐cellulose chromatography, selective precipitation and gel filtration. The 72000‐Mr DNA‐binding protein is phosphorylated and the phosphate is covalently linked predominantly to serine. Analysis of tryptic digests of the 32P‐labeled 72000‐Mr protein showed that the phosphate residue(s) is present in only one peptide. The DNA‐binding fraction contains an additional non‐phosphorylated protein with an approximate molecular weight of 45000. Tryptic peptide maps of [35S]methionine‐labeled 72000‐Mr and 45000‐Mr polypeptides are indistinguishable. The amino acid compositions of the 72000‐Mr and 45000‐Mr polypeptides show closely related distributions. An antiserum produced against the purified 72000‐Mr DNA‐binding protein precipitates both the 72000‐Mr and the 45000‐Mr protein from extracts of adenovirus‐infected cells. Immunofluorescence studies revealed DNA‐binding protein to be accumulated in characteristic structures in nuclei of the infected cells.

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“…Many researchers over the course of the last 10 years have led their studies to the identification (Rosemberg et al, 1972;Porcellati, 1963;Bridgers, 1967) and distribution (Porcellati, 1964;Ansel and Chojnacki, 1966;Forsberg et al, 1969;Rask et aL, 1970;Hubscher, 1962;Knox et al, 1969) of several amino compounds including ¿-serine and its phosphoester in the tissues of a variety of animals. Recently, it was pointed out that phosphoserine may play an important role in the phospholipid synthesis in the microsomes of the central nervous system cells (Pirotta and Guazzoni, 1971;Porcellati et al, 1970;Arienti et al, 1970).…”

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confidence: 99%

Influence of Phosphoserine on the Performance of Rats on the Rotarod

Fanelli¹

1976

Pharmacology

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The anti-fatigue effect of phosphoserine, L-serine and a mixture of sodium phosphate and L-serine has been studied in rats. Phosphoserine orally administered induced a statistically significant anti-fatigue effect in rats of both sexes submitted to a training test by rotarod, with 14 sessions in 3 days. Furthermore, phosphoserine was utilized better than the mixture of sodium phosphate and L-serine, whereas L-serine alone induced no effect. Therefore, the effect of phosphoserine seems to be due to the phosphoryl bond.

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Protein-bound phosphorylserine in different tissues and organisms

Cited by 23 publications

References 5 publications

Methyl-esterified proteins in a mammalian cell line

Methyl-esterified proteins in a mammalian cell line

Purification and Characterization of the Phosphorylated DNA-Binding Protein from Adenovirus-Type-2-Infected Cells

Influence of Phosphoserine on the Performance of Rats on the Rotarod

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