Ribonucleotide Reductase Requires Subunit Switching in Hypoxia to Maintain DNA Replication.
Ribonucleotide Reductase Requires Subunit Switching in Hypoxia to Maintain DNA Replication.
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DOI:
10.1016/j.molcel.2017.03.005
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发表时间:
2017-04-20
期刊:
影响因子:
16
通讯作者:
Hammond EM
中科院分区:
文献类型:
--
作者:
Foskolou IP;Jorgensen C;Leszczynska KB;Olcina MM;Tarhonskaya H;Haisma B;D'Angiolella V;Myers WK;Domene C;Flashman E;Hammond EM
Cells exposed to hypoxia experience replication stress but do not accumulate DNA damage, suggesting sustained DNA replication. Ribonucleotide reductase (RNR) is the only enzyme capable of de novo synthesis of deoxyribonucleotide triphosphates (dNTPs). However, oxygen is an essential cofactor for mammalian RNR (RRM1/RRM2 and RRM1/RRM2B), leading us to question the source of dNTPs in hypoxia. Here, we show that the RRM1/RRM2B enzyme is capable of retaining activity in hypoxia and therefore is favored over RRM1/RRM2 in order to preserve ongoing replication and avoid the accumulation of DNA damage. We found two distinct mechanisms by which RRM2B maintains hypoxic activity and identified responsible residues in RRM2B. The importance of RRM2B in the response to tumor hypoxia is further illustrated by correlation of its expression with a hypoxic signature in patient samples and its roles in tumor growth and radioresistance. Our data provide mechanistic insight into RNR biology, highlighting RRM2B as a hypoxic-specific, anti-cancer therapeutic target. RRM2B is induced in response to hypoxia in both cell models and patient datasets RRM2B retains activity in hypoxic conditions and is the favored RNR subunit in hypoxia Loss of RRM2B has detrimental consequences for cell fate, specifically in hypoxia RRM2B depletion enhanced hypoxic-specific apoptosis and increased radiosensitivity Foskolou et al. demonstrate that in hypoxic conditions the small subunit of the RNR enzyme is switched from RRM2 to RRM2B in order to facilitate nucleotide production and ongoing replication. They identify specific residues within RRM2B that are responsible for maintaining activity in hypoxia.