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