5gnj
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/MYC2_ARATH MYC2_ARATH] Transcriptional activator. Common transcription factor of light, abscisic acid (ABA), and jasmonic acid (JA) signaling pathways. With MYC3 and MYC4, controls additively subsets of JA-dependent responses. In cooperation with MYB2 is involved in the regulation of ABA-inducible genes under drought stress conditions. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the MYC recognition site (5'-CACATG-3'), and to the G-box (5'-CACNTG-3') and Z-box (5'-ATACGTGT-3') of promoters. Binds directly to the promoters of the transcription factors PLETHORA1 (PLT1) and PLT2 and represses their expression. Negative regulator of blue light-mediated photomorphogenic growth and blue- and far-red-light regulated gene expression. Activates multiple TIFY/JAZ promoters. Positive regulator of lateral root formation. Regulates sesquiterpene biosynthesis. Subjected to proteasome-dependent proteolysis. The presence of the destruction element (DE) involved in turnover is required for the function to regulate gene transcription.<ref>PMID:12509522</ref> <ref>PMID:15208388</ref> <ref>PMID:15923349</ref> <ref>PMID:21321051</ref> <ref>PMID:21335373</ref> <ref>PMID:21954460</ref> <ref>PMID:22669881</ref> <ref>PMID:23142764</ref> <ref>PMID:23593022</ref> <ref>PMID:23943862</ref> <ref>PMID:9368419</ref> | [https://www.uniprot.org/uniprot/MYC2_ARATH MYC2_ARATH] Transcriptional activator. Common transcription factor of light, abscisic acid (ABA), and jasmonic acid (JA) signaling pathways. With MYC3 and MYC4, controls additively subsets of JA-dependent responses. In cooperation with MYB2 is involved in the regulation of ABA-inducible genes under drought stress conditions. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the MYC recognition site (5'-CACATG-3'), and to the G-box (5'-CACNTG-3') and Z-box (5'-ATACGTGT-3') of promoters. Binds directly to the promoters of the transcription factors PLETHORA1 (PLT1) and PLT2 and represses their expression. Negative regulator of blue light-mediated photomorphogenic growth and blue- and far-red-light regulated gene expression. Activates multiple TIFY/JAZ promoters. Positive regulator of lateral root formation. Regulates sesquiterpene biosynthesis. Subjected to proteasome-dependent proteolysis. The presence of the destruction element (DE) involved in turnover is required for the function to regulate gene transcription.<ref>PMID:12509522</ref> <ref>PMID:15208388</ref> <ref>PMID:15923349</ref> <ref>PMID:21321051</ref> <ref>PMID:21335373</ref> <ref>PMID:21954460</ref> <ref>PMID:22669881</ref> <ref>PMID:23142764</ref> <ref>PMID:23593022</ref> <ref>PMID:23943862</ref> <ref>PMID:9368419</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Jasmonates (JAs) are essential plant hormones that play important roles in the regulation of plant growth and the response to environmental stress. In the JA signaling pathway, the core transcription factors are a class of basic helix-loop-helix (bHLH) proteins, including MYC2, MYC3, and MYC4, that have different regulatory capacities. Here, we report the 2.7 A crystal structure of the MYC2 bHLH domain complexed with G-box DNA, showing a cis-tetrameric structure. Biochemical assays confirmed that full-length MYC2 forms a stable homo-tetramer both in solution and in DNA-bound states, whereas MYC3 forms only a homodimer. Isothermal titration calorimetry (ITC) assays demonstrated that tetramerization enhanced DNA binding affinity, and fluorescence resonance energy transfer (FRET) assay indicated DNA looping potential of tetrameric MYC2. Luciferase assay further confirmed the importance of tetramerization in transcriptional regulation. Our studies provide a mechanistic explanation for the regulatory differences of MYC transcription factors. | ||
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| - | Crystal Structure of Tetrameric Arabidopsis MYC2 Reveals the Mechanism of Enhanced Interaction with DNA.,Lian TF, Xu YP, Li LF, Su XD Cell Rep. 2017 May 16;19(7):1334-1342. doi: 10.1016/j.celrep.2017.04.057. PMID:28514654<ref>PMID:28514654</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
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| - | <div class="pdbe-citations 5gnj" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Structure of a transcription factor and DNA complex
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