4c6r

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Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance protein RPS4Crystal structure of the TIR domain from the Arabidopsis Thaliana disease resistance protein RPS4

Structural highlights

4c6r is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.05Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPS4_ARATH Disease resistance (R) protein that specifically recognizes the AvrRps4 type III effector avirulence protein from P.syringae (PubMed:10571887, PubMed:15469494, PubMed:19519800). Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein (PubMed:10571887, PubMed:15469494, PubMed:19519800). That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (PubMed:10571887, PubMed:15469494, PubMed:19519800). Probably acts as a NAD(+) hydrolase (NADase): in response to activation, catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide; NAD(+) cleavage triggering a defense system that promotes cell death (PubMed:31439792, PubMed:31439793). The combined presence of both regular and alternative RPS4 transcripts with truncated open reading frames (ORFs) is necessary for function (PubMed:17951452). RPS4 function is regulated at multiple levels, including gene expression, alternative splicing, and protein stability (PubMed:17951452). When over-expressed, confers temperature-conditioned EDS1-dependent auto-immunity (PubMed:24146667). Heterodimerization with RRS1 is required to form a functional complex to recognize AvrRps4 and PopP2 (PubMed:24744375). Abscisic acid deficiency enhances nuclear accumulation of RPS4 and its cell death-inducing activity (PubMed:22454454).[1] [2] [3] [4] [5] [6] [7] [8] [9] [10] [11]

Publication Abstract from PubMed

Cytoplasmic plant immune receptors recognize specific pathogen effector proteins and initiate effector-triggered immunity. In Arabidopsis, the immune receptors RPS4 and RRS1 are both required to activate defense to three different pathogens. We show that RPS4 and RRS1 physically associate. Crystal structures of the N-terminal Toll-interleukin-1 receptor/resistance (TIR) domains of RPS4 and RRS1, individually and as a heterodimeric complex (respectively at 2.05, 1.75, and 2.65 angstrom resolution), reveal a conserved TIR/TIR interaction interface. We show that TIR domain heterodimerization is required to form a functional RRS1/RPS4 effector recognition complex. The RPS4 TIR domain activates effector-independent defense, which is inhibited by the RRS1 TIR domain through the heterodimerization interface. Thus, RPS4 and RRS1 function as a receptor complex in which the two components play distinct roles in recognition and signaling.

Structural basis for assembly and function of a heterodimeric plant immune receptor.,Williams SJ, Sohn KH, Wan L, Bernoux M, Sarris PF, Segonzac C, Ve T, Ma Y, Saucet SB, Ericsson DJ, Casey LW, Lonhienne T, Winzor DJ, Zhang X, Coerdt A, Parker JE, Dodds PN, Kobe B, Jones JD Science. 2014 Apr 18;344(6181):299-303. doi: 10.1126/science.1247357. PMID:24744375[12]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Gassmann W, Hinsch ME, Staskawicz BJ. The Arabidopsis RPS4 bacterial-resistance gene is a member of the TIR-NBS-LRR family of disease-resistance genes. Plant J. 1999 Nov;20(3):265-77. PMID:10571887
  2. ↑ Kwon SI, Koczan JM, Gassmann W. Two Arabidopsis srfr (suppressor of rps4-RLD) mutants exhibit avrRps4-specific disease resistance independent of RPS4. Plant J. 2004 Nov;40(3):366-75. doi: 10.1111/j.1365-313X.2004.02213.x. PMID:15469494 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02213.x
  3. ↑ Zhang XC, Gassmann W. Alternative splicing and mRNA levels of the disease resistance gene RPS4 are induced during defense responses. Plant Physiol. 2007 Dec;145(4):1577-87. doi: 10.1104/pp.107.108720. Epub 2007 Oct, 19. PMID:17951452 doi:http://dx.doi.org/10.1104/pp.107.108720
  4. ↑ Narusaka M, Shirasu K, Noutoshi Y, Kubo Y, Shiraishi T, Iwabuchi M, Narusaka Y. RRS1 and RPS4 provide a dual Resistance-gene system against fungal and bacterial pathogens. Plant J. 2009 Oct;60(2):218-26. doi: 10.1111/j.1365-313X.2009.03949.x. Epub 2009 , Jun 9. PMID:19519800 doi:http://dx.doi.org/10.1111/j.1365-313X.2009.03949.x
  5. ↑ Mang HG, Qian W, Zhu Y, Qian J, Kang HG, Klessig DF, Hua J. Abscisic acid deficiency antagonizes high-temperature inhibition of disease resistance through enhancing nuclear accumulation of resistance proteins SNC1 and RPS4 in Arabidopsis. Plant Cell. 2012 Mar;24(3):1271-84. doi: 10.1105/tpc.112.096198. Epub 2012 Mar, 27. PMID:22454454 doi:http://dx.doi.org/10.1105/tpc.112.096198
  6. ↑ Heidrich K, Tsuda K, Blanvillain-Baufume S, Wirthmueller L, Bautor J, Parker JE. Arabidopsis TNL-WRKY domain receptor RRS1 contributes to temperature-conditioned RPS4 auto-immunity. Front Plant Sci. 2013 Oct 17;4:403. doi: 10.3389/fpls.2013.00403. eCollection, 2013. PMID:24146667 doi:http://dx.doi.org/10.3389/fpls.2013.00403
  7. ↑ Williams SJ, Sohn KH, Wan L, Bernoux M, Sarris PF, Segonzac C, Ve T, Ma Y, Saucet SB, Ericsson DJ, Casey LW, Lonhienne T, Winzor DJ, Zhang X, Coerdt A, Parker JE, Dodds PN, Kobe B, Jones JD. Structural basis for assembly and function of a heterodimeric plant immune receptor. Science. 2014 Apr 18;344(6181):299-303. doi: 10.1126/science.1247357. PMID:24744375 doi:http://dx.doi.org/10.1126/science.1247357
  8. ↑ Horsefield S, Burdett H, Zhang X, Manik MK, Shi Y, Chen J, Qi T, Gilley J, Lai JS, Rank MX, Casey LW, Gu W, Ericsson DJ, Foley G, Hughes RO, Bosanac T, von Itzstein M, Rathjen JP, Nanson JD, Boden M, Dry IB, Williams SJ, Staskawicz BJ, Coleman MP, Ve T, Dodds PN, Kobe B. NAD(+) cleavage activity by animal and plant TIR domains in cell death pathways. Science. 2019 Aug 23;365(6455):793-799. doi: 10.1126/science.aax1911. PMID:31439792 doi:http://dx.doi.org/10.1126/science.aax1911
  9. ↑ Wan L, Essuman K, Anderson RG, Sasaki Y, Monteiro F, Chung EH, Osborne Nishimura E, DiAntonio A, Milbrandt J, Dangl JL, Nishimura MT. TIR domains of plant immune receptors are NAD(+)-cleaving enzymes that promote cell death. Science. 2019 Aug 23;365(6455):799-803. doi: 10.1126/science.aax1771. PMID:31439793 doi:http://dx.doi.org/10.1126/science.aax1771
  10. ↑ Zhang XC, Gassmann W. Alternative splicing and mRNA levels of the disease resistance gene RPS4 are induced during defense responses. Plant Physiol. 2007 Dec;145(4):1577-87. doi: 10.1104/pp.107.108720. Epub 2007 Oct, 19. PMID:17951452 doi:http://dx.doi.org/10.1104/pp.107.108720
  11. ↑ Narusaka M, Shirasu K, Noutoshi Y, Kubo Y, Shiraishi T, Iwabuchi M, Narusaka Y. RRS1 and RPS4 provide a dual Resistance-gene system against fungal and bacterial pathogens. Plant J. 2009 Oct;60(2):218-26. doi: 10.1111/j.1365-313X.2009.03949.x. Epub 2009 , Jun 9. PMID:19519800 doi:http://dx.doi.org/10.1111/j.1365-313X.2009.03949.x
  12. ↑ Williams SJ, Sohn KH, Wan L, Bernoux M, Sarris PF, Segonzac C, Ve T, Ma Y, Saucet SB, Ericsson DJ, Casey LW, Lonhienne T, Winzor DJ, Zhang X, Coerdt A, Parker JE, Dodds PN, Kobe B, Jones JD. Structural basis for assembly and function of a heterodimeric plant immune receptor. Science. 2014 Apr 18;344(6181):299-303. doi: 10.1126/science.1247357. PMID:24744375 doi:http://dx.doi.org/10.1126/science.1247357

4c6r, resolution 2.05Å

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