2020
DOI: 10.1074/jbc.ra120.012950
|View full text |Cite
|
Sign up to set email alerts
|

Spectral and photochemical diversity of tandem cysteine cyanobacterial phytochromes

Abstract: The atypical trichromatic cyanobacterial phytochrome NpTP1 from Nostoc punctiforme ATCC 29133 is a linear tetrapyrrole (bilin)-binding photoreceptor protein that possesses tandem-cysteine residues responsible for shifting its light-sensing maximum to the violet spectral region. Using bioinformatics and phylogenetic analyses, here we established that tandem-cysteine cyanobacterial phytochromes (TCCPs) compose a well-supported monophyletic phytochrome lineage distinct from prototypical red/far-red cyanobacterial… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

0
6
0

Year Published

2020
2020
2024
2024

Publication Types

Select...
5
1
1

Relationship

0
7

Authors

Journals

citations
Cited by 8 publications
(6 citation statements)
references
References 64 publications
0
6
0
Order By: Relevance
“…They undergo reversible photoconversion between two distinct light-absorbing states triggered by C15-Z/C15-E photoisomerization of the bilin chromophore (7,8). Phytochromes are distributed in higher plants, algae, bacteria, and fungi; they typically photoconvert between a red-absorbing C15-Z,anti dark state and a far-red lightabsorbing C15-E,anti photoproduct state, although recent studies have revealed substantial spectral diversity in some algal and cyanobacterial phytochromes (9,10). CBCRs are widely distributed among the cyanobacteria phylum and show marked variation in their absorbing wavelength, spanning the near-ultraviolet to the far-red part of the spectrum (reviewed recently in refs.…”
mentioning
confidence: 99%
“…They undergo reversible photoconversion between two distinct light-absorbing states triggered by C15-Z/C15-E photoisomerization of the bilin chromophore (7,8). Phytochromes are distributed in higher plants, algae, bacteria, and fungi; they typically photoconvert between a red-absorbing C15-Z,anti dark state and a far-red lightabsorbing C15-E,anti photoproduct state, although recent studies have revealed substantial spectral diversity in some algal and cyanobacterial phytochromes (9,10). CBCRs are widely distributed among the cyanobacteria phylum and show marked variation in their absorbing wavelength, spanning the near-ultraviolet to the far-red part of the spectrum (reviewed recently in refs.…”
mentioning
confidence: 99%
“…Cyanobacterial proteins contain the accompanying regions PAS-GAF-PHY [48]. Entire genome sequencing of cyanobacterial species, for example, Microcoleus IPAS B373 [49], Euhalothece Z-M001 [44], and Tolypothrix PCC7910 [50] are devoid of gene HY2, for phytochromobilin (PФB) synthase. Further, these cyanobacteria have pcyA gene that encodes phycocyanobilin (PCB): ferredoxin oxidoreductase that catalyzes the conversion of biliverdin (BV) to PCB, a significant cofactor of Cphs and CBCRs [32,51].…”
Section: Photosensitive Features Of Cbcr 41 Color Sensing By Cphs and Cbcrsmentioning
confidence: 99%
“…Recently, a new group of cyanobacterial PAS-GAF-PHY-composed proteins from, e.g., Nostoc punctiforme ATCC29133 (the first one in this group) were reported to carry a second cysteine capable of modifying the PCB chromophore by attachment to position 10 (see Figure 2). 15 This enzymatic bilin conversion resembles the reactivity found in CBCRs and generates remarkably blue-shifted absorption bands. We thus split the subgroup of canonical, cyanobacterial phytochromes into one represented by Cph1 (and orthologs) and a second one named TCCP (tandem cysteine cyanobacterial Phys).…”
Section: Introductionmentioning
confidence: 99%