Crystallization of a Complex Between MYC and Jas Motif

Methods Mol Biol. 2020:2085:133-144. doi: 10.1007/978-1-0716-0142-6_10.

Abstract

In the jasmonate signaling pathway, a region of 17 amino acids within the Jas motif of JAZ proteins and a conserved region within the N-terminus of MYC proteins are sufficient for JAZ-MYC interactions. Crystal structures of Jas-MYC complexes have revealed the structural basis of this important interaction. Here, we describe methods of cloning, expression, and purification of MYC N-terminal proteins and their co-crystallization with Jas motif peptides.

Keywords: Crystallization; JAZ transcription repressor; Jas motif; Jasmonate; MYC transcription factor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / chemistry
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / genetics
  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors / metabolism
  • Cloning, Molecular
  • Crystallization*
  • Gene Expression
  • Multiprotein Complexes / chemistry*
  • Multiprotein Complexes / metabolism
  • Proto-Oncogene Proteins c-myc / chemistry*
  • Proto-Oncogene Proteins c-myc / genetics*
  • Proto-Oncogene Proteins c-myc / metabolism
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Repressor Proteins / chemistry*
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism

Substances

  • Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
  • Multiprotein Complexes
  • Proto-Oncogene Proteins c-myc
  • Recombinant Proteins
  • Repressor Proteins