| Structural highlights
Function
[RCD1_ARATH] Inactive ADP-ribosyltransferase that functions with SRO1 to regulate oxidative stress, hormonal and developmental responses. Required for embryogenesis, vegetative and reproductive development, and abiotic stress responses. May regulate several stress-responsive genes. Seems to play a larger developmental role than SRO1. Does not bind NAD in vitro.[1] [2] [3] [4] [5] [6] [7] [8] [9] [10]
Publication Abstract from PubMed
Communication within cells relies on a few protein nodes called hubs, which organize vast interactomes with many partners. Frequently, hub proteins are intrinsically disordered conferring multi-specificity and dynamic communication. Conversely, folded hub proteins may organize networks using disordered partners. In this work, the structure of the RST domain, a unique folded hub, is solved by nuclear magnetic resonance spectroscopy and small-angle X-ray scattering, and its complex with a region of the transcription factor DREB2A is provided through data-driven HADDOCK modeling and mutagenesis analysis. The RST fold is unique, but similar structures are identified in the PAH (paired amphipathic helix), TAFH (TATA-box-associated factor homology), and NCBD (nuclear coactivator binding domain) domains. We designate them as a group the alphaalpha hubs, as they share an alphaalpha-hairpin super-secondary motif, which serves as an organizing platform for malleable helices of varying topology. This allows for partner adaptation, exclusion, and selection. Our findings provide valuable insights into structural features enabling signaling fidelity.
Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alphaalpha-Scaffold for Disorder in Transcriptional Networks.,Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB Structure. 2018 Apr 12. pii: S0969-2126(18)30094-7. doi:, 10.1016/j.str.2018.03.013. PMID:29657132[11]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Belles-Boix E, Babiychuk E, Van Montagu M, Inze D, Kushnir S. CEO1, a new protein from Arabidopsis thaliana, protects yeast against oxidative damage. FEBS Lett. 2000 Sep 29;482(1-2):19-24. PMID:11018516
- ↑ Overmyer K, Tuominen H, Kettunen R, Betz C, Langebartels C, Sandermann H Jr, Kangasjarvi J. Ozone-sensitive arabidopsis rcd1 mutant reveals opposite roles for ethylene and jasmonate signaling pathways in regulating superoxide-dependent cell death. Plant Cell. 2000 Oct;12(10):1849-62. PMID:11041881
- ↑ Fujibe T, Saji H, Arakawa K, Yabe N, Takeuchi Y, Yamamoto KT. A methyl viologen-resistant mutant of Arabidopsis, which is allelic to ozone-sensitive rcd1, is tolerant to supplemental ultraviolet-B irradiation. Plant Physiol. 2004 Jan;134(1):275-85. Epub 2003 Dec 4. PMID:14657410 doi:https://dx.doi.org/10.1104/pp.103.033480
- ↑ Ahlfors R, Lang S, Overmyer K, Jaspers P, Brosche M, Tauriainen A, Kollist H, Tuominen H, Belles-Boix E, Piippo M, Inze D, Palva ET, Kangasjarvi J. Arabidopsis RADICAL-INDUCED CELL DEATH1 belongs to the WWE protein-protein interaction domain protein family and modulates abscisic acid, ethylene, and methyl jasmonate responses. Plant Cell. 2004 Jul;16(7):1925-37. Epub 2004 Jun 18. PMID:15208394 doi:https://dx.doi.org/10.1105/tpc.021832
- ↑ Overmyer K, Brosche M, Pellinen R, Kuittinen T, Tuominen H, Ahlfors R, Keinanen M, Saarma M, Scheel D, Kangasjarvi J. Ozone-induced programmed cell death in the Arabidopsis radical-induced cell death1 mutant. Plant Physiol. 2005 Mar;137(3):1092-104. Epub 2005 Feb 22. PMID:15728341 doi:https://dx.doi.org/10.1104/pp.104.055681
- ↑ Fujibe T, Saji H, Watahiki MK, Yamamoto KT. Overexpression of the RADICAL-INDUCED CELL DEATH1 (RCD1) gene of Arabidopsis causes weak rcd1 phenotype with compromised oxidative-stress responses. Biosci Biotechnol Biochem. 2006 Aug;70(8):1827-31. PMID:16926493 doi:https://dx.doi.org/10.1271/bbb.50673
- ↑ Jaspers P, Blomster T, Brosche M, Salojarvi J, Ahlfors R, Vainonen JP, Reddy RA, Immink R, Angenent G, Turck F, Overmyer K, Kangasjarvi J. Unequally redundant RCD1 and SRO1 mediate stress and developmental responses and interact with transcription factors. Plant J. 2009 Oct;60(2):268-79. doi: 10.1111/j.1365-313X.2009.03951.x. Epub 2009 , Jun 22. PMID:19548978 doi:https://dx.doi.org/10.1111/j.1365-313X.2009.03951.x
- ↑ Teotia S, Lamb RS. The paralogous genes RADICAL-INDUCED CELL DEATH1 and SIMILAR TO RCD ONE1 have partially redundant functions during Arabidopsis development. Plant Physiol. 2009 Sep;151(1):180-98. doi: 10.1104/pp.109.142786. Epub 2009 Jul , 22. PMID:19625634 doi:https://dx.doi.org/10.1104/pp.109.142786
- ↑ Jaspers P, Overmyer K, Wrzaczek M, Vainonen JP, Blomster T, Salojarvi J, Reddy RA, Kangasjarvi J. The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants. BMC Genomics. 2010 Mar 12;11:170. doi: 10.1186/1471-2164-11-170. PMID:20226034 doi:https://dx.doi.org/10.1186/1471-2164-11-170
- ↑ Teotia S, Lamb RS. RCD1 and SRO1 are necessary to maintain meristematic fate in Arabidopsis thaliana. J Exp Bot. 2011 Jan;62(3):1271-84. doi: 10.1093/jxb/erq363. Epub 2010 Dec 13. PMID:21172813 doi:https://dx.doi.org/10.1093/jxb/erq363
- ↑ Bugge K, Staby L, Kemplen KR, O'Shea C, Bendsen SK, Jensen MK, Olsen JG, Skriver K, Kragelund BB. Structure of Radical-Induced Cell Death1 Hub Domain Reveals a Common alphaalpha-Scaffold for Disorder in Transcriptional Networks. Structure. 2018 Apr 12. pii: S0969-2126(18)30094-7. doi:, 10.1016/j.str.2018.03.013. PMID:29657132 doi:https://dx.doi.org/10.1016/j.str.2018.03.013
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