Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Wei Ge; Alexander Wolf; Tianshu Feng; Chia-hua Ho; Rok Sekirnik; Adam Zayer; Nicolas Granatino; Matthew E Cockman; Christoph Loenarz; Nikita D Loik; Adam P Hardy; Timothy D W Claridge; Refaat B Hamed; Rasheduzzaman Chowdhury; Lingzhi Gong; Carol V Robinson; David C Trudgian; Miao Jiang; Mukram M Mackeen; James S McCullagh; Yuliya Gordiyenko; Armin Thalhammer; Atsushi Yamamoto; Ming Yang; Phebee Liu-Yi; Zhihong Zhang; Marion Schmidt-Zachmann; Benedikt M Kessler; Peter J Ratcliffe; Gail M Preston; Mathew L Coleman; Christopher J Schofield

doi:10.1038/nchembio.1093

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Wei Ge, Alexander Wolf, Tianshu Feng, Chia-hua Ho, Rok Sekirnik, Adam Zayer, Nicolas Granatino, Matthew E Cockman, Christoph Loenarz, Nikita D Loik, Adam P Hardy, Timothy D W Claridge, Refaat B Hamed, Rasheduzzaman Chowdhury, Lingzhi Gong, Carol V Robinson, David C Trudgian, Miao Jiang, Mukram M Mackeen, James S McCullaghYuliya Gordiyenko, Armin Thalhammer, Atsushi Yamamoto, Ming Yang, Phebee Liu-Yi, Zhihong Zhang, Marion Schmidt-Zachmann, Benedikt M Kessler, Peter J Ratcliffe, Gail M Preston, Mathew L Coleman, Christopher J Schofield

Cancer and Genomic Sciences

Research output: Contribution to journal › Article › peer-review

98 Citations (Scopus)

Abstract

The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.

Original language	English
Pages (from-to)	960-2
Number of pages	3
Journal	Nature Chemical Biology
Volume	8
Issue number	12
DOIs	https://doi.org/10.1038/nchembio.1093
Publication status	Published - Dec 2012

Keywords

Animals
Arginine
Chromosomal Proteins, Non-Histone
Enzyme Inhibitors
Escherichia coli
Histidine
Humans
Hydroxylation
Magnetic Resonance Spectroscopy
Nuclear Proteins
Oxygenases
Prokaryotic Cells
Ribosomal Proteins
Ribosomes

Access to Document

10.1038/nchembio.1093

Cite this

Ge, W., Wolf, A., Feng, T., Ho, C., Sekirnik, R., Zayer, A., Granatino, N., Cockman, M. E., Loenarz, C., Loik, N. D., Hardy, A. P., Claridge, T. D. W., Hamed, R. B., Chowdhury, R., Gong, L., Robinson, C. V., Trudgian, D. C., Jiang, M., Mackeen, M. M., ... Schofield, C. J. (2012). Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. Nature Chemical Biology, 8(12), 960-2. https://doi.org/10.1038/nchembio.1093

@article{ddf52c10569d4c6e88e40ac2f12e083a,

title = "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans",

abstract = "The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.",

keywords = "Animals, Arginine, Chromosomal Proteins, Non-Histone, Enzyme Inhibitors, Escherichia coli, Histidine, Humans, Hydroxylation, Magnetic Resonance Spectroscopy, Nuclear Proteins, Oxygenases, Prokaryotic Cells, Ribosomal Proteins, Ribosomes",

author = "Wei Ge and Alexander Wolf and Tianshu Feng and Chia-hua Ho and Rok Sekirnik and Adam Zayer and Nicolas Granatino and Cockman, {Matthew E} and Christoph Loenarz and Loik, {Nikita D} and Hardy, {Adam P} and Claridge, {Timothy D W} and Hamed, {Refaat B} and Rasheduzzaman Chowdhury and Lingzhi Gong and Robinson, {Carol V} and Trudgian, {David C} and Miao Jiang and Mackeen, {Mukram M} and McCullagh, {James S} and Yuliya Gordiyenko and Armin Thalhammer and Atsushi Yamamoto and Ming Yang and Phebee Liu-Yi and Zhihong Zhang and Marion Schmidt-Zachmann and Kessler, {Benedikt M} and Ratcliffe, {Peter J} and Preston, {Gail M} and Coleman, {Mathew L} and Schofield, {Christopher J}",

year = "2012",

month = dec,

doi = "10.1038/nchembio.1093",

language = "English",

volume = "8",

pages = "960--2",

journal = "Nature Chemical Biology",

issn = "1552-4450",

publisher = "Nature Publishing Group",

number = "12",

}

Ge, W, Wolf, A, Feng, T, Ho, C, Sekirnik, R, Zayer, A, Granatino, N, Cockman, ME, Loenarz, C, Loik, ND, Hardy, AP, Claridge, TDW, Hamed, RB, Chowdhury, R, Gong, L, Robinson, CV, Trudgian, DC, Jiang, M, Mackeen, MM, McCullagh, JS, Gordiyenko, Y, Thalhammer, A, Yamamoto, A, Yang, M, Liu-Yi, P, Zhang, Z, Schmidt-Zachmann, M, Kessler, BM, Ratcliffe, PJ, Preston, GM, Coleman, ML & Schofield, CJ 2012, 'Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans', Nature Chemical Biology, vol. 8, no. 12, pp. 960-2. https://doi.org/10.1038/nchembio.1093

TY - JOUR

T1 - Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

AU - Ge, Wei

AU - Wolf, Alexander

AU - Feng, Tianshu

AU - Ho, Chia-hua

AU - Sekirnik, Rok

AU - Zayer, Adam

AU - Granatino, Nicolas

AU - Cockman, Matthew E

AU - Loenarz, Christoph

AU - Loik, Nikita D

AU - Hardy, Adam P

AU - Claridge, Timothy D W

AU - Hamed, Refaat B

AU - Chowdhury, Rasheduzzaman

AU - Gong, Lingzhi

AU - Robinson, Carol V

AU - Trudgian, David C

AU - Jiang, Miao

AU - Mackeen, Mukram M

AU - McCullagh, James S

AU - Gordiyenko, Yuliya

AU - Thalhammer, Armin

AU - Yamamoto, Atsushi

AU - Yang, Ming

AU - Liu-Yi, Phebee

AU - Zhang, Zhihong

AU - Schmidt-Zachmann, Marion

AU - Kessler, Benedikt M

AU - Ratcliffe, Peter J

AU - Preston, Gail M

AU - Coleman, Mathew L

AU - Schofield, Christopher J

PY - 2012/12

Y1 - 2012/12

N2 - The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.

AB - The finding that oxygenase-catalyzed protein hydroxylation regulates animal transcription raises questions as to whether the translation machinery and prokaryotic proteins are analogously modified. Escherichia coli ycfD is a growth-regulating 2-oxoglutarate oxygenase catalyzing arginyl hydroxylation of the ribosomal protein Rpl16. Human ycfD homologs, Myc-induced nuclear antigen (MINA53) and NO66, are also linked to growth and catalyze histidyl hydroxylation of Rpl27a and Rpl8, respectively. This work reveals new therapeutic possibilities via oxygenase inhibition and by targeting modified over unmodified ribosomes.

KW - Animals

KW - Arginine

KW - Chromosomal Proteins, Non-Histone

KW - Enzyme Inhibitors

KW - Escherichia coli

KW - Histidine

KW - Humans

KW - Hydroxylation

KW - Magnetic Resonance Spectroscopy

KW - Nuclear Proteins

KW - Oxygenases

KW - Prokaryotic Cells

KW - Ribosomal Proteins

KW - Ribosomes

U2 - 10.1038/nchembio.1093

DO - 10.1038/nchembio.1093

M3 - Article

C2 - 23103944

SN - 1552-4450

VL - 8

SP - 960

EP - 962

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 12

ER -

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Abstract

Keywords

Access to Document

Fingerprint

Cite this