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A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein.

Publication ,  Journal Article
Melotto, M; Mecey, C; Niu, Y; Chung, HS; Katsir, L; Yao, J; Zeng, W; Thines, B; Staswick, P; Browse, J; Howe, GA; He, SY
Published in: The Plant journal : for cell and molecular biology
September 2008

Coronatine is an important virulence factor produced by several pathovars of the bacterial pathogen Pseudomonas syringae. The structure of coronatine is similar to that of a class of plant hormones called jasmonates (JAs). An important step in JA signaling is the SCF(COI1) E3 ubiquitin ligase-dependent degradation of JAZ repressor proteins. We have recently shown that jasmonoyl isoleucine (JA-Ile) promotes physical interaction between Arabidopsis JAZ1 and COI1 (the F-box component of SCF(COI1)) proteins, and that the JA-Ile-dependent COI1-JAZ1 interaction could be reconstituted in yeast cells (i.e. in the absence of other plant proteins). Here we show that coronatine, but not its two biosynthetic precursors, also promotes interaction between Arabidopsis COI1 and multiple JAZ proteins. The C-terminal Jas motif, but not the N-terminal (NT) domain or central ZIM domain of JAZ proteins, is critical for JA-Ile/coronatine-dependent interaction with COI1. Two positively charged amino acid residues in the Jas domain were identified as essential for coronatine-dependent COI1-JAZ interactions. Mutations of these two residues did not affect the ability of JAZ1 and JAZ9 to interact with the transcription factor AtMYC2. Importantly, transgenic Arabidopsis plants expressing JAZ1 carrying these two mutations exhibited JA-insensitive phenotypes, including male sterility and enhanced resistance to P. syringae infection. These results not only suggest that coronatine and JA-Ile target the physical interaction between COI1 and the Jas domain of JAZ repressors, but also illustrate the critical role of positively charged amino acids in the Jas domain in mediating the JA-Ile/coronatine-dependent JAZ interaction with COI1.

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Published In

The Plant journal : for cell and molecular biology

DOI

EISSN

1365-313X

ISSN

0960-7412

Publication Date

September 2008

Volume

55

Issue

6

Start / End Page

979 / 988

Related Subject Headings

  • Two-Hybrid System Techniques
  • Saccharomyces cerevisiae
  • Repressor Proteins
  • Pseudomonas syringae
  • Pseudomonas Infections
  • Protein Interaction Domains and Motifs
  • Plants, Genetically Modified
  • Plant Growth Regulators
  • Plant Diseases
  • Plant Biology & Botany
 

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Melotto, M., Mecey, C., Niu, Y., Chung, H. S., Katsir, L., Yao, J., … He, S. Y. (2008). A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein. The Plant Journal : For Cell and Molecular Biology, 55(6), 979–988. https://doi.org/10.1111/j.1365-313x.2008.03566.x
Melotto, Maeli, Christy Mecey, Yajie Niu, Hoo Sun Chung, Leron Katsir, Jian Yao, Weiqing Zeng, et al. “A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein.The Plant Journal : For Cell and Molecular Biology 55, no. 6 (September 2008): 979–88. https://doi.org/10.1111/j.1365-313x.2008.03566.x.
Melotto M, Mecey C, Niu Y, Chung HS, Katsir L, Yao J, et al. A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein. The Plant journal : for cell and molecular biology. 2008 Sep;55(6):979–88.
Melotto, Maeli, et al. “A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein.The Plant Journal : For Cell and Molecular Biology, vol. 55, no. 6, Sept. 2008, pp. 979–88. Epmc, doi:10.1111/j.1365-313x.2008.03566.x.
Melotto M, Mecey C, Niu Y, Chung HS, Katsir L, Yao J, Zeng W, Thines B, Staswick P, Browse J, Howe GA, He SY. A critical role of two positively charged amino acids in the Jas motif of Arabidopsis JAZ proteins in mediating coronatine- and jasmonoyl isoleucine-dependent interactions with the COI1 F-box protein. The Plant journal : for cell and molecular biology. 2008 Sep;55(6):979–988.
Journal cover image

Published In

The Plant journal : for cell and molecular biology

DOI

EISSN

1365-313X

ISSN

0960-7412

Publication Date

September 2008

Volume

55

Issue

6

Start / End Page

979 / 988

Related Subject Headings

  • Two-Hybrid System Techniques
  • Saccharomyces cerevisiae
  • Repressor Proteins
  • Pseudomonas syringae
  • Pseudomonas Infections
  • Protein Interaction Domains and Motifs
  • Plants, Genetically Modified
  • Plant Growth Regulators
  • Plant Diseases
  • Plant Biology & Botany