Nicole Frankenberg‐Dinkel

Rheinland-Pfälzische Technische Universität Kaiserslautern-Landau

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

Eckhard Hofmann

Ruhr University Bochum

Michelle M. Gehringer

Rheinland-Pfälzische Technische Universität Kaiserslautern-Landau

Dirk W. Heinz

University of Applied Sciences Ravensburg-Weingarten

Dieter Jahn

Technische Universität Braunschweig

Thorben Dammeyer

Technische Universität Braunschweig

J. Clark Lagarias

University of California, Davis

Kerstin Fiege

Royal Netherlands Institute for Sea Research

Susanne Zehner

University of Koblenz and Landau

Benjamin Ledermann

University of Kaiserslautern

F. Frère

University of Zurich

Cooperative Institutions

University of Kaiserslautern

Ruhr University Bochum

Rheinland-Pfälzische Technische Universität Kaiserslautern-Landau

Max Planck Society

University of Koblenz and Landau

Technische Universität Braunschweig

Technische Universität Berlin

University of Freiburg

Humboldt-Universität zu Berlin

Karlsruhe Institute of Technology

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

Bacterial Heme Oxygenases

Antioxidants and Redox Signaling (2004)

Nicole Frankenberg‐Dinkel

The importance of heme oxygenases in heme catabolism, iron utilization, and cellular signaling has been recognized for many years and is a well studied process in eukaryotes. Through the accessibility of an increasing number of bacterial genomes, it has become evident that heme oxygenases are also widespread in prokaryotes. In these organisms, the heme oxygenase reaction serves a similar function as in eukaryotes. A major role of bacterial heme oxygenases has been attributed to acquisition of iron in prokaryotic pathogens, but other functions, such as involvement in phytobilin biosynthesis, have been described. This review summarizes the current state of the art on bacterial heme oxygenase research. The various biological roles of this enzyme in prokaryotes and their biochemical properties will be discussed. Antioxid. Redox Signal. 6, 825–834.

10.1089/ars.2004.6.825

Cite

Citations (107)

Early‐Branching Cyanobacteria Grow Faster and Upregulate Superoxide Dismutase Activity Under a Simulated Early Earth Anoxic Atmosphere

Geobiology (2024)

Sadia S. Tamanna Joanne S. Boden Kimberly Michelle Kaiser Nicola Wannicke Jonas Hoering

ABSTRACT The evolution of oxygenic photosynthesis during the Archean (4–2.5 Ga) required the presence of complementary reducing pathways to maintain the cellular redox balance. While the timing of the evolution of superoxide dismutases (SODs), enzymes that convert superoxide to hydrogen peroxide and O 2 , within bacteria and archaea is not resolved, the first SODs appearing in cyanobacteria contained copper and zinc in the reaction center (CuZnSOD). Here, we analyse growth characteristics, SOD gene expression (qRT‐PCR) and cellular enzyme activity in the deep branching strain, Pseudanabaena sp. PCC7367, previously demonstrated to release significantly more O 2 under anoxic conditions. The observed significantly higher growth rates ( p < 0.001) and protein and glycogen contents ( p < 0.05) in anoxically cultured Pseudanabaena PCC7367 compared to control cultures grown under present‐day oxygen‐rich conditions prompted the following question: Is the growth of Pseudanabaena sp. PCC7367 correlated to atmospheric p O 2 and cellular SOD activity? Expression of sodB (encoding FeSOD) and sodC (encoding CuZnSOD) strongly correlated with medium O 2 levels ( p < 0.001). Expression of sodA (encoding MnSOD) correlated significantly to SOD activity during the day ( p = 0.019) when medium O 2 concentrations were the highest. The cellular SOD enzyme activity of anoxically grown cultures was significantly higher ( p < 0.001) 2 h before the onset of the dark phase compared to O 2 ‐rich growth conditions. The expression of SOD encoding genes was significantly reduced ( p < 0.05) under anoxic conditions in stirred cultures, as were medium O 2 levels ( p ≤ 0.001), compared to oxic‐grown cultures, whereas total cellular SOD activity remained comparable. Our data suggest that increasing p O 2 negatively impacts the viability of early cyanobacteria, possibly by increasing photorespiration. Additionally, the increased expression of superoxide‐inactivating genes during the dark phase suggests the increased replacement rates of SODs under modern‐day conditions compared to those on early Earth.

10.1111/gbi.70005

Cite

Citations (0)

Pink bacteria—Production of the pink chromophore phycoerythrobilin with Escherichia coli

Journal of Biotechnology (2018)

Judith Stiefelmaier Benjamin Ledermann Michael Sorg Angela Banek Doris Geib

Phycobiliprotein

10.1016/j.jbiotec.2018.03.006

Cite

Citations (17)

New biosynthetic pathway for pink pigments from uncultured oceanic viruses

Environmental Microbiology (2016)

Benjamin Ledermann Oded Béjà Nicole Frankenberg‐Dinkel

The pink open-chain tetrapyrrole pigment phycoerythrobilin (PEB) is employed by marine cyanobacteria, red algae and cryptophytes as a light-harvesting chromophore in phycobiliproteins. Genes encoding biosynthesis proteins for PEB have also been discovered in cyanophages, viruses that infect cyanobacteria, and mimic host pigment biosynthesis with the exception of PebS which combines the enzymatic activities of two host enzymes. In this study, we have identified novel members of the PEB biosynthetic enzyme families, heme oxygenases and ferredoxin-dependent bilin reductases. Encoding genes were found in metagenomic datasets and could be traced back to bacteriophage but not cyanophage origin. While the heme oxygenase exhibited standard activity, a new bilin reductase with highest homology to the teal pigment producing enzyme PcyA revealed PEB biosynthetic activity. Although PcyX possesses PebS-like activity both enzymes share only 9% sequence identity and likely catalyze the reaction via two independent mechanisms. Our data point towards the presence of phycobilin biosynthetic genes in phages that probably infect alphaproteobacteria and, therefore, further support a role of phycobilins outside oxygenic phototrophs.

Phycobiliprotein

Tetrapyrrole

10.1111/1462-2920.13290

Cite

Citations (24)

Exchange of a single amino acid residue in the cryptophyte phycobiliprotein lyaseGtCPES expands its substrate specificity

bioRxiv (Cold Spring Harbor Laboratory) (2020)

Natascha Tomazic Kristina E. Overkamp Marco Aras Antonio J. Pierik Eckhard Hofmann

ABSTRACT Cryptophyte algae are among the few eukaryotes that employ phycobiliproteins (PBP) for light harvesting during oxygenic photosynthesis. In contrast to the cyanobacterial PBP that are organized in large membrane-associated super complexes, the phycobilisomes, those from cryptophytes are soluble within the chloroplast thylakoid lumen. Their light-harvesting capacity is due to covalent linkage of several open-chain tetrapyrrole chromophores (phycobilins). Guillardia theta utilizes the PBP phycoerythrin PE545 with 15,16-dihydrobiliverdin (DHBV) in addition to phycoerythrobilin (PEB) as chromophores. Thus far, the assembly of cryptophyte PBPs is not yet completely understood but involves the action of PBP-lyases as shown for cyanobacterial PBP. PBP-lyases facilitate the attachment of the chromophore in the right configuration and stereochemistry. Here we present the functional characterization of eukaryotic S-type PBP lyase Gt CPES from G. theta . We show Gt CPES mediated transfer and covalent attachment of PEB to the conserved Cys 82 of the acceptor PBP β-subunit ( Pm CpeB) of Prochlorococcus marinus MED4. Based on the previously solved crystal structure, the Gt CPES binding pocket was investigated using site-directed mutagenesis. Thereby, amino acid residues involved in phycobilin binding and transfer were identified. Interestingly, exchange of a single amino acid residue Met 67 to Ala extended the substrate specificity to phycocyanobilin (PCB) likely by enlarging the substrate-binding pocket. Variant Gt CPES_M67A binds both PEB and PCB forming a stable, colorful complex in vitro and in vivo produced in Escherichia coli . Gt CPES_M67A is able to mediate PCB transfer to Cys 82 of Pm CpeB. Based on our data we postulate that a single amino acid residue determines the bilin-specificity of phycoerythrin S-type lyases but that additional factors regulate hand over to the target protein.

Phycobiliprotein

Phycocyanobilin

Phycobilisome

Lyase

10.1101/2020.03.31.018853

Cite

Citations (1)

A light regulated OmpR‐class promoter element co‐ordinates light‐harvesting protein and chromophore biosynthetic enzyme gene expression

Molecular Microbiology (2007)

Richard M. Alvey Ryan P. Bezy Nicole Frankenberg‐Dinkel David M. Kehoe

Summary Co‐ordination of chromophore and apoprotein biosynthesis is required during photosynthetic light‐harvesting antennae production, such as occurs during complementary chromatic adaptation (CCA). This response to ambient light colour changes is controlled by a phytochrome‐class photoreceptor and involves changes in the synthesis of cyanobacterial light‐harvesting antennae. During growth in red light, CCA activates cpc2 transcription, an operon that encodes the light‐harvesting protein phycocyanin. In order to function, this apoprotein must have covalently attached phycocyanobilin chromophores, which are synthesized by PcyA. We show that pcyA is also transcriptionally activated by CCA during red light growth and is not regulated via feedback that senses cpc2 RNA levels. The pcyA and cpc2 promoters contain a common regulatory element, a direct repeat typical of OmpR‐class transcription factor binding sites, at similar positions relative to their red light‐controlled transcription start sites. Deletion of this element from the pcyA promoter eliminated CCA‐regulated transcription, and insertion of the element into a non‐light responsive promoter conferred CCA regulation. We conclude that this element is necessary and sufficient to confer CCA transcriptional regulation and that it co‐ordinates phycocyanin and phycocyanobilin biosynthesis in red light.

Phycocyanobilin

Phytochrome

Transcription

Biliverdin

10.1111/j.1365-2958.2007.05656.x

Cite

Citations (25)

The Arabidopsis HY2 Gene Encodes Phytochromobilin Synthase, a Ferredoxin-Dependent Biliverdin Reductase

The Plant Cell (2001)

Takayuki Kohchi Keiko Mukougawa Nicole Frankenberg‐Dinkel Munehisa Masuda Akiho Yokota

Biliverdin reductase

Biliverdin

Glutamate synthase

Ferredoxin—NADP(+) reductase

10.2307/3871286

Cite

Citations (14)

Efficient Phage-Mediated Pigment Biosynthesis in Oceanic Cyanobacteria

Current Biology (2008)

Thorben Dammeyer Sarah C. Bagby Matthew B. Sullivan Sallie W. Chisholm Nicole Frankenberg‐Dinkel

10.1016/j.cub.2008.02.067

Cite

Citations (182)

Spectroscopic characterization of the heme binding (GAF) domain of two sensor kinases from Methanosarcina acetivorans

WORLD SCIENTIFIC eBooks (2020)

Kerstin Fiege Christian Twittenhoff Kathrin Kwiatkowski Nicole Frankenberg‐Dinkel

Characterization

10.1142/9789811223556_0113

Cite

Citations (0)

Darkness inhibits autokinase activity of bacterial bathy phytochromes

Journal of Biological Chemistry (2024)

Christina Huber Merle Strack Isabel Schultheiß Julia Pielage Xenia Mechler

Bathy phytochromes are a subclass of bacterial biliprotein photoreceptors that carry a biliverdin IXα chromophore. In contrast to prototypical phytochromes that adopt a red-light absorbing Pr ground state, the far-red light absorbing Pfr-form is the thermally stable ground state of bathy phytochromes. Although the photobiology of bacterial phytochromes has been extensively studied since their discovery in the late 1990s, our understanding of the signal transduction process to the connected transmitter domains, which are often histidine kinases, remains insufficient. Initiated by the analysis of the bathy phytochrome PaBphP from Pseudomonas aeruginosa, we performed a systematic analysis of five different bathy phytochromes with the aim to derive a general statement on the correlation of photostate and autokinase output. While all proteins adopt different Pr/Pfr-fractions in response to red, blue, and far-red light, only darkness leads to a pure or highly-enriched Pfr-form, directly correlated with the lowest level of autokinase activity. Using this information, we developed a method to quantitatively correlate the autokinase activity of phytochrome samples with well-defined stationary Pr/Pfr-fractions. We demonstrate that the off-state of the phytochromes is the Pfr-form and that different Pr/Pfr-fractions enable the organisms to fine-tune their kinase output in response to a certain light environment. Furthermore, the output response is regulated by the rate of dark reversion, which differs significantly from 5 seconds to 50 minutes half-life. Overall, our study indicates that bathy phytochromes function as sensors of light and darkness, rather than red and far-red light, as originally postulated.

Darkness

Phytochrome

10.1016/j.jbc.2024.107148

Cite

Citations (1)