Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms. / Nestoras, Konstantinos; Mohammed, Asma Hadi; Schreurs, Ann-Sofie; Fleck, Oliver; Watson, Adam T; Poitelea, Marius; O'Shea, Charlotte; Chahwan, Charly; Holmberg, Christian; Kragelund, Birthe B; Nielsen, Olaf; Osborne, Mark; Carr, Antony M; Liu, Cong.

In: Genes & Development, Vol. 24, No. 11, 01.06.2010, p. 1145-1159.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Nestoras, K, Mohammed, AH, Schreurs, A-S, Fleck, O, Watson, AT, Poitelea, M, O'Shea, C, Chahwan, C, Holmberg, C, Kragelund, BB, Nielsen, O, Osborne, M, Carr, AM & Liu, C 2010, 'Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms', Genes & Development, vol. 24, no. 11, pp. 1145-1159. https://doi.org/10.1101/gad.561910

APA

Nestoras, K., Mohammed, A. H., Schreurs, A-S., Fleck, O., Watson, A. T., Poitelea, M., O'Shea, C., Chahwan, C., Holmberg, C., Kragelund, B. B., Nielsen, O., Osborne, M., Carr, A. M., & Liu, C. (2010). Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms. Genes & Development, 24(11), 1145-1159. https://doi.org/10.1101/gad.561910

Vancouver

Nestoras K, Mohammed AH, Schreurs A-S, Fleck O, Watson AT, Poitelea M et al. Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms. Genes & Development. 2010 Jun 1;24(11):1145-1159. https://doi.org/10.1101/gad.561910

Author

Nestoras, Konstantinos ; Mohammed, Asma Hadi ; Schreurs, Ann-Sofie ; Fleck, Oliver ; Watson, Adam T ; Poitelea, Marius ; O'Shea, Charlotte ; Chahwan, Charly ; Holmberg, Christian ; Kragelund, Birthe B ; Nielsen, Olaf ; Osborne, Mark ; Carr, Antony M ; Liu, Cong. / Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms. In: Genes & Development. 2010 ; Vol. 24, No. 11. pp. 1145-1159.

Bibtex

@article{83fb7802f5604046bfdfcb53c35562f7,
title = "Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms",
abstract = "The correct levels of deoxyribonucleotide triphosphates and their relative abundance are important to maintain genomic integrity. Ribonucleotide reductase (RNR) regulation is complex and multifaceted. RNR is regulated allosterically by two nucleotide-binding sites, by transcriptional control, and by small inhibitory proteins that associate with the R1 catalytic subunit. In addition, the subcellular localization of the R2 subunit is regulated through the cell cycle and in response to DNA damage. We show that the fission yeast small RNR inhibitor Spd1 is intrinsically disordered and regulates R2 nuclear import, as predicted by its relationship to Saccharomyces cerevisiae Dif1. We demonstrate that Spd1 can interact with both R1 and R2, and show that the major restraint of RNR in vivo by Spd1 is unrelated to R2 subcellular localization. Finally, we identify a new behavior for RNR complexes that potentially provides yet another mechanism to regulate dNTP synthesis via modulation of RNR complex architecture.",
keywords = "Active Transport, Cell Nucleus, Alanine, Cell Cycle Proteins, Gene Expression Regulation, Fungal, Mutagenesis, Protein Subunits, Ribonucleotide Reductases, Schizosaccharomyces, Schizosaccharomyces pombe Proteins",
author = "Konstantinos Nestoras and Mohammed, {Asma Hadi} and Ann-Sofie Schreurs and Oliver Fleck and Watson, {Adam T} and Marius Poitelea and Charlotte O'Shea and Charly Chahwan and Christian Holmberg and Kragelund, {Birthe B} and Olaf Nielsen and Mark Osborne and Carr, {Antony M} and Cong Liu",
year = "2010",
month = jun,
day = "1",
doi = "10.1101/gad.561910",
language = "English",
volume = "24",
pages = "1145--1159",
journal = "Genes & Development",
issn = "0890-9369",
publisher = "Cold Spring Harbor Laboratory Press",
number = "11",

}

RIS

TY - JOUR

T1 - Regulation of ribonucleotide reductase by Spd1 involves multiple mechanisms

AU - Nestoras, Konstantinos

AU - Mohammed, Asma Hadi

AU - Schreurs, Ann-Sofie

AU - Fleck, Oliver

AU - Watson, Adam T

AU - Poitelea, Marius

AU - O'Shea, Charlotte

AU - Chahwan, Charly

AU - Holmberg, Christian

AU - Kragelund, Birthe B

AU - Nielsen, Olaf

AU - Osborne, Mark

AU - Carr, Antony M

AU - Liu, Cong

PY - 2010/6/1

Y1 - 2010/6/1

N2 - The correct levels of deoxyribonucleotide triphosphates and their relative abundance are important to maintain genomic integrity. Ribonucleotide reductase (RNR) regulation is complex and multifaceted. RNR is regulated allosterically by two nucleotide-binding sites, by transcriptional control, and by small inhibitory proteins that associate with the R1 catalytic subunit. In addition, the subcellular localization of the R2 subunit is regulated through the cell cycle and in response to DNA damage. We show that the fission yeast small RNR inhibitor Spd1 is intrinsically disordered and regulates R2 nuclear import, as predicted by its relationship to Saccharomyces cerevisiae Dif1. We demonstrate that Spd1 can interact with both R1 and R2, and show that the major restraint of RNR in vivo by Spd1 is unrelated to R2 subcellular localization. Finally, we identify a new behavior for RNR complexes that potentially provides yet another mechanism to regulate dNTP synthesis via modulation of RNR complex architecture.

AB - The correct levels of deoxyribonucleotide triphosphates and their relative abundance are important to maintain genomic integrity. Ribonucleotide reductase (RNR) regulation is complex and multifaceted. RNR is regulated allosterically by two nucleotide-binding sites, by transcriptional control, and by small inhibitory proteins that associate with the R1 catalytic subunit. In addition, the subcellular localization of the R2 subunit is regulated through the cell cycle and in response to DNA damage. We show that the fission yeast small RNR inhibitor Spd1 is intrinsically disordered and regulates R2 nuclear import, as predicted by its relationship to Saccharomyces cerevisiae Dif1. We demonstrate that Spd1 can interact with both R1 and R2, and show that the major restraint of RNR in vivo by Spd1 is unrelated to R2 subcellular localization. Finally, we identify a new behavior for RNR complexes that potentially provides yet another mechanism to regulate dNTP synthesis via modulation of RNR complex architecture.

KW - Active Transport, Cell Nucleus

KW - Alanine

KW - Cell Cycle Proteins

KW - Gene Expression Regulation, Fungal

KW - Mutagenesis

KW - Protein Subunits

KW - Ribonucleotide Reductases

KW - Schizosaccharomyces

KW - Schizosaccharomyces pombe Proteins

U2 - 10.1101/gad.561910

DO - 10.1101/gad.561910

M3 - Journal article

C2 - 20516199

VL - 24

SP - 1145

EP - 1159

JO - Genes & Development

JF - Genes & Development

SN - 0890-9369

IS - 11

ER -

ID: 33576513