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5t0f

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Crystal structure of the Myc3 N-terminal domain [44-242] in complex with JAZ10 CMID domain [16-58] from arabidopsis

Structural highlights

5t0f is a 2 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 2.4Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MYC3_ARATH Transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. With MYC2 and MYC4, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.^[1] ^[2] ^[3] ^[4] ^[5]

Publication Abstract from PubMed

Jasmonate ZIM-domain (JAZ) transcriptional repressors play a key role in regulating jasmonate (JA) signaling in plants. Below a threshold concentration of jasmonoyl isoleucine (JA-Ile), the active form of JA, the C-terminal Jas motif of JAZ proteins binds MYC transcription factors to repress JA signaling. With increasing JA-Ile concentration, the Jas motif binds to JA-Ile and the COI1 subunit of the SCFCOI1 E3 ligase, which mediates ubiquitination and proteasomal degradation of JAZ repressors, resulting in derepression of MYC transcription factors. JA signaling subsequently becomes desensitized, in part by feedback induction of JAZ splice variants that lack the C-terminal Jas motif but include an N-terminal cryptic MYC-interaction domain (CMID). The CMID sequence is dissimilar to the Jas motif and is incapable of recruiting SCFCOI1, allowing CMID-containing JAZ splice variants to accumulate in the presence of JA and to re-repress MYC transcription factors as an integral part of reestablishing signal homeostasis. The mechanism by which the CMID represses MYC transcription factors remains elusive. Here we describe the crystal structure of the MYC3-CMIDJAZ10 complex. In contrast to the Jas motif, which forms a single continuous helix when bound to MYC3, the CMID adopts a loop-helix-loop-helix architecture with modular interactions with both the Jas-binding groove and the backside of the Jas-interaction domain of MYC3. This clamp-like interaction allows the CMID to bind MYC3 tightly and block access of MED25 (a subunit of the Mediator coactivator complex) to the MYC3 transcriptional activation domain, shedding light on the enigmatic mechanism by which JAZ splice variants desensitize JA signaling.

Structural insights into alternative splicing-mediated desensitization of jasmonate signaling.,Zhang F, Ke J, Zhang L, Chen R, Sugimoto K, Howe GA, Xu HE, Zhou M, He SY, Melcher K Proc Natl Acad Sci U S A. 2017 Feb 14;114(7):1720-1725. doi:, 10.1073/pnas.1616938114. Epub 2017 Jan 30. PMID:28137867^[6]

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

References

↑ Smolen GA, Pawlowski L, Wilensky SE, Bender J. Dominant alleles of the basic helix-loop-helix transcription factor ATR2 activate stress-responsive genes in Arabidopsis. Genetics. 2002 Jul;161(3):1235-46. PMID:12136026
↑ Cheng Z, Sun L, Qi T, Zhang B, Peng W, Liu Y, Xie D. The bHLH transcription factor MYC3 interacts with the Jasmonate ZIM-domain proteins to mediate jasmonate response in Arabidopsis. Mol Plant. 2011 Mar;4(2):279-88. doi: 10.1093/mp/ssq073. Epub 2011 Jan 17. PMID:21242320 doi:http://dx.doi.org/10.1093/mp/ssq073
↑ Niu Y, Figueroa P, Browse J. Characterization of JAZ-interacting bHLH transcription factors that regulate jasmonate responses in Arabidopsis. J Exp Bot. 2011 Mar;62(6):2143-54. doi: 10.1093/jxb/erq408. Epub 2011 Feb 14. PMID:21321051 doi:http://dx.doi.org/10.1093/jxb/erq408
↑ Fernandez-Calvo P, Chini A, Fernandez-Barbero G, Chico JM, Gimenez-Ibanez S, Geerinck J, Eeckhout D, Schweizer F, Godoy M, Franco-Zorrilla JM, Pauwels L, Witters E, Puga MI, Paz-Ares J, Goossens A, Reymond P, De Jaeger G, Solano R. The Arabidopsis bHLH transcription factors MYC3 and MYC4 are targets of JAZ repressors and act additively with MYC2 in the activation of jasmonate responses. Plant Cell. 2011 Feb;23(2):701-15. doi: 10.1105/tpc.110.080788. Epub 2011 Feb 18. PMID:21335373 doi:http://dx.doi.org/10.1105/tpc.110.080788
↑ Schweizer F, Fernandez-Calvo P, Zander M, Diez-Diaz M, Fonseca S, Glauser G, Lewsey MG, Ecker JR, Solano R, Reymond P. Arabidopsis basic helix-loop-helix transcription factors MYC2, MYC3, and MYC4 regulate glucosinolate biosynthesis, insect performance, and feeding behavior. Plant Cell. 2013 Aug;25(8):3117-32. doi: 10.1105/tpc.113.115139. Epub 2013 Aug, 13. PMID:23943862 doi:http://dx.doi.org/10.1105/tpc.113.115139
↑ Zhang F, Ke J, Zhang L, Chen R, Sugimoto K, Howe GA, Xu HE, Zhou M, He SY, Melcher K. Structural insights into alternative splicing-mediated desensitization of jasmonate signaling. Proc Natl Acad Sci U S A. 2017 Feb 14;114(7):1720-1725. doi:, 10.1073/pnas.1616938114. Epub 2017 Jan 30. PMID:28137867 doi:http://dx.doi.org/10.1073/pnas.1616938114

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5t0f"

@@ Line 3: / Line 3: @@
 <StructureSection load='5t0f' size='340' side='right'caption='[[5t0f]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5t0f]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T0F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T0F FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5t0f]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T0F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T0F FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rru|4rru]], [[4rqw|4rqw]], [[4rs9|4rs9]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYC3, ATR2, BHLH5, EN36, At5g46760, MZA15.18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), TIFY9, JAS1, JAZ10, At5g13220, T31B5.40 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t0f OCA], [https://pdbe.org/5t0f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t0f RCSB], [https://www.ebi.ac.uk/pdbsum/5t0f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t0f ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t0f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t0f OCA], [http://pdbe.org/5t0f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t0f RCSB], [http://www.ebi.ac.uk/pdbsum/5t0f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t0f ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MYC3_ARATH MYC3_ARATH]] Transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. With MYC2 and MYC4, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.<ref>PMID:12136026</ref> <ref>PMID:21242320</ref> <ref>PMID:21321051</ref> <ref>PMID:21335373</ref> <ref>PMID:23943862</ref>  [[http://www.uniprot.org/uniprot/TIF9_ARATH TIF9_ARATH]] Modulator of growth inhibition. Isoform 2 and isoform 3, but not isoform 1, confer a strong methyl-jasmonate insensitivity. Not involved in the growth response to salicylic acid or indole-3-acetic acid. Isoform 3 acts as an endogenous repressor of JA signal output in JA-stimulated cells (PubMed:19151223).<ref>PMID:17675405</ref> <ref>PMID:19151223</ref> <ref>PMID:23632853</ref>
+[https://www.uniprot.org/uniprot/MYC3_ARATH MYC3_ARATH] Transcription factor involved in tryptophan, jasmonic acid (JA) and other stress-responsive gene regulation. With MYC2 and MYC4, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.<ref>PMID:12136026</ref> <ref>PMID:21242320</ref> <ref>PMID:21321051</ref> <ref>PMID:21335373</ref> <ref>PMID:23943862</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
 [[Category: Large Structures]]
-[[Category: Brunzelle, J S]]
+[[Category: Brunzelle JS]]
-[[Category: He, S Y]]
+[[Category: He SY]]
-[[Category: Ke, J]]
+[[Category: Ke J]]
-[[Category: Melcher, K]]
+[[Category: Melcher K]]
-[[Category: Xu, H E]]
+[[Category: Xu HE]]
-[[Category: Zhang, F]]
+[[Category: Zhang F]]
-[[Category: Alternative splicing]]
-[[Category: Desensitization]]
-[[Category: Jasmonate signaling]]
-[[Category: Jaz10 cmid]]
-[[Category: Myc3]]
-[[Category: Transcription]]
-[[Category: Transcriptional repression]]

5t0f

From Proteopedia

Current revision

Crystal structure of the Myc3 N-terminal domain [44-242] in complex with JAZ10 CMID domain [16-58] from arabidopsis

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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