Phytochromes and bacterial sensor proteins are related by structural and functional homologies Hypothesis on phytochrome‐mediated signal‐transduction

Schneider‐Poetsch, Hansjörg A. W.; Braun, Birgit; Marx, Stefan; Schaumburg, Anke

doi:10.1016/0014-5793(91)80403-p

Cited by 105 publications

(63 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Evidence of hotnologues in prokaryotes is limited, though similarity atnong the C-termini of phytochromes and the histidine kinase domains of bacterial two-component response regulators has been noted (e.g. Schneider-Poetsch et al 1991). The strongest support for comtnon ancestry comes from characterization of a phytochrome-like putative photoreceptor frotn the cyanobacterium Fremyella (Kehoe & Grossman 1996) and frotn sequence analysis of the genotne of Synechocystis strain PCC 6803 (Kaneko et al 1995).…”

Section: Diversification Of the Phytochrome Gene Family During The Evmentioning

confidence: 99%

Phytochrome gene diversity

Mathews

Sharrock

1997

Plant Cell & Environment

265

214

View full text Add to dashboard Cite

The structures and functions of the phytochrome apoprotein genes (the PHY genes), their diversity across the plant kingdom, and their evolution are central concerns in the study of red-light sensing in plants. We summarize here recent advances in two areas relating to these topics: (1) the characteristics of the PHY gene family in Arabidopsis thaliana, the higher plant species for which the most extensive information on these genes is available, and (2) the similarity relationships, phylogeny, and evolutionary implications of PHY gene sequences and partial sequences which have been described from various plants. Together, these two areas of study, one directed at understanding in detail the phytochromes present in a single species and the other directed at a much broader understanding of PHY gene relatedness and distribution, are producing an increasingly clear picture of the diversity and evolution of plant red-light photoreceptors. Moreover, they suggest that the complexity of the phytochrome family has increased as land plants have evolved novel morphologies.

show abstract

Section: Diversification Of the Phytochrome Gene Family During The Evmentioning

confidence: 99%

Phytochrome gene diversity

Mathews

Sharrock

1997

Plant Cell & Environment

265

214

View full text Add to dashboard Cite

show abstract

“…Missense mutations located in these motifs cause impaired light responses (Xu et al, 1995;Yanovsky et al, 2002). Similar to other PHYs, the distant C-terminal part of the PHYA molecule contains the His kinase-related domain, which shows homology to bacterial His kinases (Schneider-Poetsch et al, 1991;Yeh and Lagarias, 1998;Montgomery and Lagarias, 2002). The C-terminal domains of PHYA and PHYB are involved in mediating interaction with several proteins (Ni et al, 1998;Choi et al, 1999;Fankhauser et al, 1999) and in phytochrome nuclear import (Mü ller et al, 2009).…”

mentioning

confidence: 99%

Missense Mutation in the Amino Terminus of Phytochrome A Disrupts the Nuclear Import of the Photoreceptor

et al. 2011

View full text Add to dashboard Cite

Phytochromes are the red/far-red photoreceptors in higher plants. Among them, phytochrome A (PHYA) is responsible for the far-red high-irradiance response and for the perception of very low amounts of light, initiating the very-low-fluence response. Here, we report a detailed physiological and molecular characterization of the phyA-5 mutant of Arabidopsis (Arabidopsis thaliana), which displays hyposensitivity to continuous low-intensity far-red light and shows reduced very-low-fluence response and high-irradiance response. Red light-induced degradation of the mutant phyA-5 protein appears to be normal, yet higher residual amounts of phyA-5 are detected in seedlings grown under low-intensity far-red light. We show that (1) the phyA-5 mutant harbors a new missense mutation in the PHYA amino-terminal extension domain and that (2) the complex phenotype of the mutant is caused by reduced nuclear import of phyA-5 under low fluences of far-red light. We also demonstrate that impaired nuclear import of phyA-5 is brought about by weakened binding affinity of the mutant photoreceptor to nuclear import facilitators FHY1 (for FAR-RED ELONGATED HYPOCOTYL1) and FHL (for FHY1-LIKE). Finally, we provide evidence that the signaling and degradation kinetics of constitutively nuclear-localized phyA-5 and phyA are identical. Taken together, our data show that aberrant nucleo/cytoplasmic distribution impairs light-induced degradation of this photoreceptor and that the amino-terminal extension domain mediates the formation of the FHY1/FHL/PHYA far-redabsorbing form complex, whereby it plays a role in regulating the nuclear import of phyA.

show abstract

“…We have provisionally called the new phytochrome gene CpPHY2. The 3Ј coding region of CpPHY2 is homologous to the catalytic domain of two-component transmitter histidine kinases, a typical feature of conventional-type phytochromes (Schneider-Poetsch et al, 1991;Thü mmler et al, 1995a) and exhibits about 85% nucleotide sequence identity to conventional-type phytochrome from the moss Physcomitrella (X75025; Kolukisaoglu et al, 1993). ZAPc23 also represents a 5Ј-truncated cDNA clone (Figure 1).…”

Section: Isolation Of Ceratodon Phytochrome Cdna Clonesmentioning

confidence: 99%

“…With the exception of a phytochrome species in the moss Ceratodon purpureus (CpPHY1, see below), the C-termini of all other phytochromes exhibit homology to the catalytic domain of protein histidine kinases (conventional phytochrome). The latter constitute the environmental sensor proteins of bacteria, suggesting that phytochrome acts as a light-regulated protein kinase (Schneider-Poetsch, 1991;Thü mmler et al, 1995a). This proposal has received strong support due to the recent identification of genes homologous to phytochrome in cyanobacteria which also exhibit the canonical motifs of the catalytic domain of histidine kinases within their C-terminal regions (Kaneko et al, 1996;Kehoe and Grossman, 1996).…”

Section: Introductionmentioning

confidence: 98%

Characterization and expression of the phytochrome gene family in the moss Ceratodon purpureus

Pasentsis¹,

Paulo²,

Algarra³

et al. 1998

The Plant Journal

View full text Add to dashboard Cite

SummaryIn the moss Ceratodon purpureus, phytochrome is encoded by two different genes, CpPHY1 and CpPHY2. CpPHY2 represents a conventional type phytochrome characterized by a C-terminus homologous to the catalytic domain of bacterial sensor histidine kinases, whereas CpPHY1 represents an unique phytochrome, which carries a C-terminus homologous to the catalytic domain of eukaryotic serine/threonine/tyrosine kinases. Southern blot analysis revealed that CpPHY1 is present in different Ceratodon cultivars which were collected in Germany and in Finland, implying that CpPHY1 represents a functional and active gene in Ceratodon, but CpPHY1 homologous genes could not be detected in another moss, Physcomitrella patens, or in Arabidopsis thaliana. cDNA analysis of CpPHY1 revealed the presence of a hitherto unnoticed intron within the 3Ј region. This results in a change of the sequence of the 11 C-terminal amino acids from KLSSHSYLTSK to FSSYQDSYPSTEELS. CpPHY1 and CpPHY2 mRNAs appear to accumulate in a light-independent manner, with CpPHY2 being much more strongly expressed than CpPHY1. Accordingly, in crude protein extracts, CpPHY2 is clearly detectable by Western blot analysis, whereas CpPHY1 is not. Light-dependent expression of CpPHY2 can be detected at the post-transcriptional level; during a 7-day period of dark adaptation, pronounced CpPHY2 accumulation occurs. Upon transfer to white light, dark-accumulated CpPHY2 is depleted within 24 h. That depletion can be completely inhibited by the photosynthesis inhibitor 3-(3,4-dichlorophenyl)-1,1-dimethyl urea (DCMU), implying that photosynthesis is strongly involved in the adjustment of phytochrome steady-state concentrations in Ceratodon. The presence of an ORF within the 5Ј UTR region of CpPHY2 (uORF) encoding peptide MKEFSSTSRSLMIVGIY suggests regulation at the translational level. The uORF resides on a short intron which is excised from the 5Ј leader in a light-dependent manner, resulting in the formation of an alternative uORF encoding peptide MEEEEDCVP.

show abstract

Phytochromes and bacterial sensor proteins are related by structural and functional homologies Hypothesis on phytochrome‐mediated signal‐transduction

Cited by 105 publications

References 28 publications

Phytochrome gene diversity

Phytochrome gene diversity

Missense Mutation in the Amino Terminus of Phytochrome A Disrupts the Nuclear Import of the Photoreceptor

Characterization and expression of the phytochrome gene family in the moss Ceratodon purpureus

Contact Info

Product

Resources

About