Jon Hughes

ORCID: 0000-0001-6070-004X
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About
Contact & Profiles
Research Areas
  • Light effects on plants
  • Photosynthetic Processes and Mechanisms
  • Plant Molecular Biology Research
  • Photoreceptor and optogenetics research
  • Algal biology and biofuel production
  • Biocrusts and Microbial Ecology
  • Plant and Biological Electrophysiology Studies
  • Plant and animal studies
  • Greenhouse Technology and Climate Control
  • Advanced NMR Techniques and Applications
  • Bryophyte Studies and Records
  • Flowering Plant Growth and Cultivation
  • Plant Genetic and Mutation Studies
  • Plant Reproductive Biology
  • Marine and coastal plant biology
  • Magnetic and Electromagnetic Effects
  • CRISPR and Genetic Engineering
  • Mine drainage and remediation techniques
  • Phytoplasmas and Hemiptera pathogens
  • RNA and protein synthesis mechanisms
  • Remote Sensing in Agriculture
  • Ecology, Conservation, and Geographical Studies
  • Chromium effects and bioremediation
  • NMR spectroscopy and applications
  • Literature and Cultural Memory

Justus-Liebig-Universität Gießen
2014-2025

Freie Universität Berlin
1998-2025

Giessen School of Theology
2015-2024

Carnegie Institution for Science
2012

Leiden University
2006-2010

University of Freiburg
1987-2007

Joint Genome Institute
2007

Lawrence Livermore National Laboratory
2007

Kanazawa University
2007

Advanced Science Research Center
2007

We report the draft genome sequence of model moss Physcomitrella patens and compare its features with those flowering plants, from which it is separated by more than 400 million years, unicellular aquatic algae. This comparison reveals genomic changes concomitant evolutionary movement to land, including a general increase in gene family complexity; loss genes associated environments (e.g., flagellar arms); acquisition for tolerating terrestrial stresses variation temperature water...

10.1126/science.1150646 article EN Science 2007-12-14

Phytochromes are red/far-red photochromic biliprotein photoreceptors, which in plants regulate seed germination, stem extension, flowering time, and many other light effects. However, the structure/functional basis of phytochrome photoswitch is still unclear. Here, we report ground state structure complete sensory module Cph1 from cyanobacterium Synechocystis 6803. Although phycocyanobilin (PCB) chromophore attached to Cys-259 as expected, paralleling situation plant phytochromes but...

10.1073/pnas.0806477105 article EN Proceedings of the National Academy of Sciences 2008-09-18

Phytochrome photoreceptors mediate light responses in plants and many microorganisms. Here we report studies using 1 H– 13 C magic-angle spinning NMR spectroscopy of the sensor module cyanobacterial phytochrome Cph1. Two isoforms red-light absorbing Pr ground state are identified. Conclusive evidence that photoisomerization occurs at C15-methine bridge leading to a β -facial disposition ring D is presented. In far-red-light Pfr state, strong hydrogen-bonding interactions -ring carbonyl group...

10.1073/pnas.1013377108 article EN Proceedings of the National Academy of Sciences 2011-02-15

The complete sequence of the Synechocystis chromosome has revealed a phytochrome-like that yielded an authentic phytochrome when overexpressed in Escherichia coli . In this paper we describe recombinant more detail. Islands strong similarity to plant phytochromes were found throughout cyanobacterial whereas C-terminal homologies identify it as likely sensory histidine kinase, family which are related. An ≈ 300 residue portion is important for function missing from sequence, immediately front...

10.1073/pnas.94.22.11792 article EN Proceedings of the National Academy of Sciences 1997-10-28

Although most plant species from algae to flowering plants use blue light for inducing phototropism and chloroplast movement, many ferns, some mosses, green red as well the regulation of these responses, resulting in better sensitivity at low levels. During their evolution, ferns have created a chimeric photoreceptor (phy3 Adiantum ) between phytochrome (phy) phototropin (phot) enabling them effectively. We identified two genes resembling PHY3 , NEOCHROME1 NEOCHROME2 ( MsNEO1 MsNEO2 ), alga...

10.1073/pnas.0504734102 article EN Proceedings of the National Academy of Sciences 2005-09-08

Phytochromes are red/far-red photochromic photoreceptors central to regulating plant development. Although they known enter the nucleus upon light activation and, once there, regulate transcription, this is not complete picture. Various phytochrome effects manifested much too rapidly derive from changes in gene expression, whereas others seem occur without entering nucleus. also guide directional responses light, excluding a genetic signaling route and implying instead plasma membrane...

10.1073/pnas.1120203109 article EN Proceedings of the National Academy of Sciences 2012-07-05

The phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803 forms holoprotein adducts with close spectral similarity to plant phytochromes when autoassembled in vitro bilin chromophores. is a 85‐kDa protein that acts as light‐regulated histidine kinase seemingly involved ‘two‐component’ signalling. This paper describes improvement of purification, estimation extinction coefficient holo‐Cph1, analyses assembly procedure and studies on quaternary structure. During natural chromophore...

10.1046/j.1432-1327.2001.02395.x article EN European Journal of Biochemistry 2001-09-01

The Pr to Pfr transition of recombinant Synechocystis PCC 6803 phytochrome Cph1 and its N-terminal sensor domain Cph1Δ2 is accompanied by net acidification in unbuffered solution. extent this photoreversible proton release was measured with a conventional pH electrode increased from less than 0.1 released per formed at 9 between 0.6 (Cph1) 1.1 (Cph1Δ2) H+/Pfr 6. kinetics the were monitored 7 8 using flash-induced transient absorption measurements indicator dye fluorescein. Proton occurs time...

10.1021/bi002651d article EN Biochemistry 2001-08-29

Both thermally stable states of phytochrome, Pr and Pfr, have been studied by (13)C (15)N cross-polarization (CP) magic-angle spinning (MAS) NMR using cyanobacterial (Cph1) plant (phyA) phytochrome sensory modules containing uniformly (13)C- (15)N-labeled bilin chromophores. Two-dimensional homo- heteronuclear experiments allowed most the chemical shifts to be assigned in both states. Chemical shift differences reflect changes electronic structure cofactor at atomic level as well its...

10.1073/pnas.0805696105 article EN Proceedings of the National Academy of Sciences 2008-10-02

Phytochromes are biological red/far-red light sensors found in many organisms. Photoisomerization of the linear methine-bridged tetrapyrrole triggers transient proton translocation events chromophore binding pocket (CBP) leading to major conformational changes protein matrix that turn associated with signaling. By combining pH-dependent resonance Raman and UV–visible absorption spectroscopy, we analyzed protonation-dependent equilibria CBP Cph1 involving proposed Pr-I Pr-II substates prevail...

10.1021/acs.jpcb.6b09600 article EN The Journal of Physical Chemistry B 2016-12-14

Prokaryotic systems have been important in phytochrome studies on several different levels. Bilins from cyanobacterial phycobiliproteins allowed the production of recombinant holophytochrome and provided insights into attachment functioning chromophore, while recent

10.1104/pp.121.4.1059 article EN PLANT PHYSIOLOGY 1999-12-01

The plant photoreceptor phytochrome plays an important role in the nucleus as a regulator of transcription. Numerous studies imply, however, that phytochromes both higher and lower plants mediate physiological reactions within cytoplasm. In particular, tip cells moss protonemal filaments use to sense light direction, requiring signaling system transmits directional information directly microfilaments direct growth. this work we describe four canonical genes model species Physcomitrella...

10.1073/pnas.0403140101 article EN Proceedings of the National Academy of Sciences 2004-09-13

Precise structural information regarding the chromophore binding pocket is essential for an understanding of photochromicity and photoconversion in phytochrome photoreceptors. To this end, we are studying 59 kDa N-terminal module cyanobacterial Cph1 from Synechocystis sp. PCC 6803 both thermally stable forms (Pr Pfr) using solution-state NMR spectroscopy. The protein deuterated, while chromophore, phycocyanobilin (PCB), isotopically labeled with 15N or 13C 15N. We have established a simple...

10.1021/bi050457r article EN Biochemistry 2005-05-21

We have investigated mutants of phytochrome Cph1 from the cyanobacterium Synechocystis PCC6803 in order to study chromophore-protein interactions. Cph1Delta2, 514-residue N-terminal sensor module produced as a recombinant His6-tagged apoprotein Escherichia coli, autoassembles vitro form holoprotein photochemically indistinguishable full-length product. generated 12 site-directed focusing on conserved residues which might be involved autoassembly and photoconversion. Folding,...

10.1111/j.1742-4658.2006.05164.x article EN FEBS Journal 2006-03-08

The cyanobacterial phytochrome Cph1 can be photoconverted between two thermally stable states, Pr and Pfr. photochemically induced Pfr --> back-reaction has been followed at low temperature by magic-angle spinning (MAS) NMR spectroscopy, allowing intermediates, Lumi-F Meta-F, to trapped. Employing uniformly (13)C- (15)N-labeled open-chain tetrapyrrole chromophores, all four states-Pfr, Lumi-F, Pr-have structurally characterized. In the first step, double bond photoisomerization forming...

10.1021/ja9108616 article EN Journal of the American Chemical Society 2010-03-05

We present structural information for oat phyA3 in the far-red-light-absorbing (Pfr) signaling state, to our knowledge first three-dimensional (3D) a plant phytochrome as Pfr. Solid-state magic-angle spinning (MAS) NMR was used detect interatomic contacts complete photosensory module [residues 1-595, including NTE (N-terminal extension), PAS (Per/Arnt/Sim), GAF (cGMP phosphodiesterase/adenylyl cyclase/FhlA) and PHY (phytochrome-specific) domains but with C-terminal repeat transmitter-like...

10.3389/fpls.2018.00498 article EN cc-by Frontiers in Plant Science 2018-04-24
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