The N-terminal fragment of arabidopsis photomorphogenic repressor COP1 maintains partial function and acts in a concentration-dependent manner

Chatanika Stoop-Myer, Keiko U. Torii, Timothy W. McNellis, Joseph E. Coleman, Xing Wang Deng

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Arabidopsis seedlings exhibit distinct developmental patterns according to their light environment: photomorphogenesis in the light and etiolation or skotomorphogenesis in darkness. COP1 acts within the nucleus to repress photomorphogenesis in darkness, while light depletes COP1 from nucleus and abrogates this repression. COP1 contains three structural modules: a RING finger followed by a coiled-coil domain, and a WD40 repeat domain at the C-terminus. By introducing various domain deletion mutants of COP1 into cop1 null mutant backgrounds, we show that all three domains are essential for the function of COP1 in vivo. Interestingly, a fragment containing the N-terminal 282 amino acids of COP1 (N282) with both the RING finger and coiled-coil modules is sufficient to rescue the lethality of the cop1 null mutations at low expression level. However, high expression levels of the N282 fragment result in a phenocopy of the cop1 null mutation. The sensitivity of the seedling to levels of N282 could reflect the importance of the abundance of COP1 for the appropriate regulation of photomorphogenic development.

Original languageEnglish (US)
Pages (from-to)713-717
Number of pages5
JournalPlant Journal
Volume20
Issue number6
DOIs
StatePublished - Dec 1999

All Science Journal Classification (ASJC) codes

  • Genetics
  • Plant Science
  • Cell Biology

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