Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets
The N-end rule pathway targets substrate proteins for proteasomal degradation. Here, Whiteet al. show that ArabidopsisPLANT CYSTEINE OXIDASEs show dioxygenase activity producing Cys-sulfinic acid at the N-terminus of target proteins, which then act as direct substrates for arginyl transferase.
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Nature Portfolio
2017
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oai:doaj.org-article:208c41197c3f40509bc868b20218a21a2021-12-02T17:06:25ZPlant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets10.1038/ncomms146902041-1723https://doaj.org/article/208c41197c3f40509bc868b20218a21a2017-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms14690https://doaj.org/toc/2041-1723The N-end rule pathway targets substrate proteins for proteasomal degradation. Here, Whiteet al. show that ArabidopsisPLANT CYSTEINE OXIDASEs show dioxygenase activity producing Cys-sulfinic acid at the N-terminus of target proteins, which then act as direct substrates for arginyl transferase.Mark D. WhiteMaria KleckerRichard J. HopkinsonDaan A. WeitsCarolin MuellerChristin NaumannRebecca O’NeillJames WickensJiayu YangJonathan C. Brooks-BartlettElspeth F. GarmanTom N. GrossmannNico DissmeyerEmily FlashmanNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-9 (2017) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
Science Q |
| spellingShingle |
Science Q Mark D. White Maria Klecker Richard J. Hopkinson Daan A. Weits Carolin Mueller Christin Naumann Rebecca O’Neill James Wickens Jiayu Yang Jonathan C. Brooks-Bartlett Elspeth F. Garman Tom N. Grossmann Nico Dissmeyer Emily Flashman Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| description |
The N-end rule pathway targets substrate proteins for proteasomal degradation. Here, Whiteet al. show that ArabidopsisPLANT CYSTEINE OXIDASEs show dioxygenase activity producing Cys-sulfinic acid at the N-terminus of target proteins, which then act as direct substrates for arginyl transferase. |
| format |
article |
| author |
Mark D. White Maria Klecker Richard J. Hopkinson Daan A. Weits Carolin Mueller Christin Naumann Rebecca O’Neill James Wickens Jiayu Yang Jonathan C. Brooks-Bartlett Elspeth F. Garman Tom N. Grossmann Nico Dissmeyer Emily Flashman |
| author_facet |
Mark D. White Maria Klecker Richard J. Hopkinson Daan A. Weits Carolin Mueller Christin Naumann Rebecca O’Neill James Wickens Jiayu Yang Jonathan C. Brooks-Bartlett Elspeth F. Garman Tom N. Grossmann Nico Dissmeyer Emily Flashman |
| author_sort |
Mark D. White |
| title |
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| title_short |
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| title_full |
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| title_fullStr |
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| title_full_unstemmed |
Plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets |
| title_sort |
plant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of n-end rule targets |
| publisher |
Nature Portfolio |
| publishDate |
2017 |
| url |
https://doaj.org/article/208c41197c3f40509bc868b20218a21a |
| work_keys_str_mv |
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1718381601810808832 |