The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis

Research output: Contribution to journalJournal articlepeer-review

Standard

The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis. / Palm, L; Andersen, J; Rahbek-Nielsen, H; Hansen, T S; Kristiansen, K; Højrup, P.

In: Journal of Biological Chemistry, Vol. 270, No. 11, 1995, p. 6000-5.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Palm, L, Andersen, J, Rahbek-Nielsen, H, Hansen, TS, Kristiansen, K & Højrup, P 1995, 'The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis', Journal of Biological Chemistry, vol. 270, no. 11, pp. 6000-5. <http://www.ncbi.nlm.nih.gov/pubmed/7890730>

APA

Palm, L., Andersen, J., Rahbek-Nielsen, H., Hansen, T. S., Kristiansen, K., & Højrup, P. (1995). The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis. Journal of Biological Chemistry, 270(11), 6000-5. http://www.ncbi.nlm.nih.gov/pubmed/7890730

Vancouver

Palm L, Andersen J, Rahbek-Nielsen H, Hansen TS, Kristiansen K, Højrup P. The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis. Journal of Biological Chemistry. 1995;270(11):6000-5.

Author

Palm, L ; Andersen, J ; Rahbek-Nielsen, H ; Hansen, T S ; Kristiansen, K ; Højrup, P. / The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 11. pp. 6000-5.

Bibtex

@article{e7e6aee00f0d11de8478000ea68e967b,
title = "The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis",
abstract = "A single basic ribosomal protein, protein S7, can be multiply phosphorylated in the ciliated protozoan Tetrahymena. Induction of phosphorylation is highly regulated, and the phosphorylation proceeds in a strictly sequential manner. The first site to be phosphorylated is a serine residue and the second a threonine. In this paper we report the complete primary structure of Tetrahymena thermophila ribosomal protein S7 including identification of the phosphorylated serine and threonine residues. Most of the sequence information was obtained from peptides generated by in situ digestion of S7 in two-dimensional gels using an approach that combined traditional protein chemistry with mass spectrometry. T. thermophila ribosomal protein S7 has a molecular mass of 29,459 Da and contains 259 amino acid residues. Phosphorylation takes place on Ser258 and Thr248 in the C-terminal region of the protein. Alignment of T. thermophila ribosomal protein S7 with known ribosomal proteins yielded the surprising result that T. thermophila S7 is homologous, not with mammalian ribosomal protein S6, but with mammalian ribosomal protein S4. These findings clearly distinguish the pattern of phosphorylation of ribosomal proteins in Tetrahymena from all other eukaryotes analyzed to date.",
author = "L Palm and J Andersen and H Rahbek-Nielsen and Hansen, {T S} and K Kristiansen and P H{\o}jrup",
note = "Keywords: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Cyanogen Bromide; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Humans; Mass Spectrometry; Methanococcus; Molecular Sequence Data; Peptide Fragments; Phosphorylation; Phosphoserine; Phosphothreonine; Rats; Ribosomal Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Tetrahymena thermophila; Trypsin",
year = "1995",
language = "English",
volume = "270",
pages = "6000--5",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "11",

}

RIS

TY - JOUR

T1 - The phosphorylated ribosomal protein S7 in Tetrahymena is homologous with mammalian S4 and the phosphorylated residues are located in the C-terminal region. Structural characterization of proteins separated by two-dimensional polyacrylamide gel electrophoresis

AU - Palm, L

AU - Andersen, J

AU - Rahbek-Nielsen, H

AU - Hansen, T S

AU - Kristiansen, K

AU - Højrup, P

N1 - Keywords: Amino Acid Sequence; Animals; Chromatography, High Pressure Liquid; Cyanogen Bromide; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Humans; Mass Spectrometry; Methanococcus; Molecular Sequence Data; Peptide Fragments; Phosphorylation; Phosphoserine; Phosphothreonine; Rats; Ribosomal Proteins; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Tetrahymena thermophila; Trypsin

PY - 1995

Y1 - 1995

N2 - A single basic ribosomal protein, protein S7, can be multiply phosphorylated in the ciliated protozoan Tetrahymena. Induction of phosphorylation is highly regulated, and the phosphorylation proceeds in a strictly sequential manner. The first site to be phosphorylated is a serine residue and the second a threonine. In this paper we report the complete primary structure of Tetrahymena thermophila ribosomal protein S7 including identification of the phosphorylated serine and threonine residues. Most of the sequence information was obtained from peptides generated by in situ digestion of S7 in two-dimensional gels using an approach that combined traditional protein chemistry with mass spectrometry. T. thermophila ribosomal protein S7 has a molecular mass of 29,459 Da and contains 259 amino acid residues. Phosphorylation takes place on Ser258 and Thr248 in the C-terminal region of the protein. Alignment of T. thermophila ribosomal protein S7 with known ribosomal proteins yielded the surprising result that T. thermophila S7 is homologous, not with mammalian ribosomal protein S6, but with mammalian ribosomal protein S4. These findings clearly distinguish the pattern of phosphorylation of ribosomal proteins in Tetrahymena from all other eukaryotes analyzed to date.

AB - A single basic ribosomal protein, protein S7, can be multiply phosphorylated in the ciliated protozoan Tetrahymena. Induction of phosphorylation is highly regulated, and the phosphorylation proceeds in a strictly sequential manner. The first site to be phosphorylated is a serine residue and the second a threonine. In this paper we report the complete primary structure of Tetrahymena thermophila ribosomal protein S7 including identification of the phosphorylated serine and threonine residues. Most of the sequence information was obtained from peptides generated by in situ digestion of S7 in two-dimensional gels using an approach that combined traditional protein chemistry with mass spectrometry. T. thermophila ribosomal protein S7 has a molecular mass of 29,459 Da and contains 259 amino acid residues. Phosphorylation takes place on Ser258 and Thr248 in the C-terminal region of the protein. Alignment of T. thermophila ribosomal protein S7 with known ribosomal proteins yielded the surprising result that T. thermophila S7 is homologous, not with mammalian ribosomal protein S6, but with mammalian ribosomal protein S4. These findings clearly distinguish the pattern of phosphorylation of ribosomal proteins in Tetrahymena from all other eukaryotes analyzed to date.

M3 - Journal article

C2 - 7890730

VL - 270

SP - 6000

EP - 6005

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 11

ER -

ID: 11231846