Cryptochrome 1, cryptochrome 2, and phytochrome a co-activate the chloroplast psbD blue light-responsive promoter.

نویسندگان

  • K E Thum
  • M Kim
  • D A Christopher
  • J E Mullet
چکیده

The reaction center core of photosystem II is composed of two chlorophyll binding proteins, D1 and D2, that are encoded by the chloroplast genes psbA and psbD. These chlorophyll binding proteins are damaged during photochemistry, especially under high irradiance. Photosystem II function is maintained under these conditions through turnover and resynthesis of D1 and D2. Blue light-activated transcription of psbD from a special light-responsive promoter is part of the repair system. In this study, light-activated chloroplast and psbD transcription were studied after dark adaptation of 21-day-old light-grown Arabidopsis plants. Illumination of dark-adapted plants with red light increased chloroplast transcription activity and transcription from the psbD light-responsive promoter. Blue light further increased chloroplast transcription activity and stimulated differential transcription from the psbD light-responsive promoter. Photoreceptor mutants showed that blue light-specific activation of chloroplast transcription and the psbD light-responsive promoter involve cryptochrome 1 (cry1) or cryptochrome 2 (cry2) and phytochrome A (phyA). Blue light-induced activation of the psbD light-responsive promoter was normal in det2-1 and hy5-1 but attenuated in det3-1. Therefore, cry1/cry2/phyA-mediated blue light activation of the psbD light-responsive promoter in 21-day-old Arabidopsis plants does not involve hy5, a transcription factor that mediates other phyA and blue light-induced responses.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Hierarchical coupling of phytochromes and cryptochromes reconciles stability and light modulation of Arabidopsis development.

In plants, development is a continuing process that takes place under strong fluctuations of the light environment. Here we show that in Arabidopsis thaliana plants grown under intense white light, coupling of the photoreceptor cryptochrome 2 to developmental processes is broader than previously appreciated. Compared to the wild type, the cry2 mutant showed reduced activity of a Lhcb1*2 promote...

متن کامل

Blue Light-Dependent Interaction of CRY2 with SPA1 Regulates COP1 activity and Floral Initiation in Arabidopsis

Cryptochromes are blue light receptors that mediate light regulation of gene expression in all major evolution lineages, but the molecular mechanism underlying cryptochrome signal transduction remains not fully understood. It has been reported that cryptochromes suppress activity of the multifunctional E3 ubiquitin ligase CONSTITUTIVE PHOTOMORPHOGENIC 1 (COP1) to regulate gene expression in res...

متن کامل

Cryptochrome, Phytochrome, and the Photoregulation of Anthocyanin Production under Blue Light.

The principle of equivalent light action predicts that two light treatments (wavelengths ;lambda(1) and lambda(2)) producing the same Pfr/P ratio (phi(lambda1) = phi(lambda2)) and the same rate of phytochrome photoconversion (k(lambda1) = k(lambda2)) are perceived by phytochrome as being the same and should produce the same effect. The results of experiments based on the principle of equivalent...

متن کامل

Chimeric proteins between cry1 and cry2 Arabidopsis blue light photoreceptors indicate overlapping functions and varying protein stability.

A blue light (cryptochrome) photoreceptor from Arabidopsis, cry1, has been identified recently and shown to mediate a number of blue light-dependent phenotypes. Similar to phytochrome, the cryptochrome photoreceptors are encoded by a gene family of homologous members with considerable amino acid sequence similarity within the N-terminal chromophore binding domain. The two members of the Arabido...

متن کامل

Molecular basis for blue light-dependent phosphorylation of Arabidopsis cryptochrome 2

Plant cryptochromes undergo blue light-dependent phosphorylation to regulate their activity and abundance, but the protein kinases that phosphorylate plant cryptochromes have remained unclear. Here we show that photoexcited Arabidopsis cryptochrome 2 (CRY2) is phosphorylated in vivo on as many as 24 different residues, including 7 major phosphoserines. We demonstrate that four closely related P...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Plant cell

دوره 13 12  شماره 

صفحات  -

تاریخ انتشار 2001