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Journal article

Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants

Abstract:

Organisms must respond to hypoxia to preserve oxygen homeostasis. We identify a thiol oxidase, previously assigned as cysteamine (2-aminoethanethiol) dioxygenase (ADO), as a low oxygen affinity (high-KmO2) amino-terminal cysteine dioxygenase that transduces the oxygen-regulated stability of proteins by the N-degron pathway in human cells. ADO catalyzes the conversion of amino-terminal cysteine to cysteine sulfinic acid and is related to the plant cysteine oxidases that mediate responses to hy...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1126/science.aaw0112

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
ORCID:
0000-0002-9714-905X
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Sub department:
Oxford Ludwig Institute
Role:
Author
ORCID:
0000-0002-0334-7144
More by this author
Role:
Author
ORCID:
0000-0003-4968-4071
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Sub department:
Organic Chemistry
Role:
Author
ORCID:
0000-0002-1431-0339
More by this author
Role:
Author
ORCID:
0000-0001-9920-9020
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Publisher:
American Association for the Advancement of Science Publisher's website
Journal:
Science Journal website
Volume:
365
Issue:
6448
Pages:
65-69
Publication date:
2019-07-05
Acceptance date:
2019-06-12
DOI:
EISSN:
1095-9203
ISSN:
0036-8075
Source identifiers:
1027215
Language:
English
Pubs id:
pubs:1027215
UUID:
uuid:e34ffb7c-0f6a-4b24-bc61-3784ad0bc253
Local pid:
pubs:1027215
Deposit date:
2019-07-05

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