The F-box protein ZEITLUPE confers dosage-dependent control on the circadian clock, photomorphogenesis, and flowering time

DE Somers, WY Kim, R Geng - The Plant Cell, 2004 - academic.oup.com
DE Somers, WY Kim, R Geng
The Plant Cell, 2004academic.oup.com
As an F-box protein, ZEITLUPE (ZTL) is involved in targeting one or more substrates for
ubiquitination and degradation via the proteasome. The initial characterization of ZTL
suggested a function limited largely to the regulation of the circadian clock. Here, we show a
considerably broader role for ZTL in the control of circadian period and
photomorphogenesis. Using a ZTL-specific antibody, we quantitated and characterized a
ZTL dosage series that ranges from a null mutation to a strong ZTL overexpressor. In the …
Abstract
As an F-box protein, ZEITLUPE (ZTL) is involved in targeting one or more substrates for ubiquitination and degradation via the proteasome. The initial characterization of ZTL suggested a function limited largely to the regulation of the circadian clock. Here, we show a considerably broader role for ZTL in the control of circadian period and photomorphogenesis. Using a ZTL-specific antibody, we quantitated and characterized a ZTL dosage series that ranges from a null mutation to a strong ZTL overexpressor. In the dark,ztl null mutations lengthen circadian period, and overexpression causes arrhythmicity, suggesting a more comprehensive role for this protein in the clock than previously suspected. In the light, circadian period becomes increasingly shorter at higher levels of ZTL, to the point of arrhythmicity. By contrast, hypocotyl length increases and flowering time is delayed in direct proportion to the level of ZTL. We propose a novel testable mechanism by which circadian period and amplitude may act together to gate phytochrome B–mediated suppression of hypocotyl. We also demonstrate that ZTL-dependent delay of flowering is mediated through decreases in CONSTANS and FLOWERING LOCUS T message levels, thus directly linking proteasome-dependent proteolysis to flowering.
Oxford University Press