Protochlorophyllide Forms in Etiolated Seedlings of Photoreceptor Mutants of Arabidopsis Thaliana — Is Chlorophyll Biosynthesis Controlled by Cooperation between Phytochromes and Phototropins?

Author(s):  
Beata Myśliwa-Kurdziel ◽  
Elżbieta Turek ◽  
Przemysław Malec
2016 ◽  
Vol 11 (8) ◽  
pp. e1214349 ◽  
Author(s):  
Edouard Boex-Fontvieille ◽  
Sachin Rustgi ◽  
Diter Von Wettstein ◽  
Stephan Pollmann ◽  
Steffen Reinbothe ◽  
...  

2001 ◽  
Vol 98 (22) ◽  
pp. 12826-12831 ◽  
Author(s):  
R. Meskauskiene ◽  
M. Nater ◽  
D. Goslings ◽  
F. Kessler ◽  
R. op den Camp ◽  
...  

1991 ◽  
Vol 97 (4) ◽  
pp. 1470-1475 ◽  
Author(s):  
Vladimir Orbović ◽  
Kenneth L. Poff

Nanomaterials ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 615
Author(s):  
Valentina Gallo ◽  
Andrea Zappettini ◽  
Marco Villani ◽  
Nelson Marmiroli ◽  
Marta Marmiroli

In previous work, two independent Arabidopsis thaliana Ac/Ds transposon insertional mutant lines, atnp01 and atnp02, were identified that showed a higher level of tolerance than the wild type (wt) line to cadmium sulfide quantum dots (CdS QDs). The tolerance response was characterized at physiological, genetic and transcriptomic levels. In this work, a comparative analysis was performed on protein extracts from plantlets of the two mutants and of wt, each treated with 80 mg L−1 CdS QDs. A comparative protein analysis was performed by 2D-PAGE, and proteins were characterized by MALDI-TOF/TOF mass spectrometry. Of 250 proteins identified from all three lines, 98 showed significant changes in relative abundance between control and CdS QD-treated plantlets. The wt, atnp01, and atnp02 control-treated pairs respectively showed 61, 31, and 31 proteins with differential expression. The two mutants had a different response to treatment in terms of type and quantity of up- and downregulated proteins. This difference became more striking when compared to wt. A network analysis of the proteins differentially expressed in atnp01 and atnp02 included several of those encoded by putative genes accommodating the transposons, which were responsible for regulation of some proteins identified in this study. These included nifu-like protein 3 (Nfu3), involved in chloroplast assembly, elongator complex 3 (Elo3), involved in transcriptional elongation, magnesium-chelate subunit-2 (Chli2), involved in chlorophyll biosynthesis, and protein phosphatase 2C (PP2C) which mediates abiotic stress response.


2009 ◽  
Vol 47 (4) ◽  
pp. 510-516 ◽  
Author(s):  
A. Pavlovic ◽  
L. Slovakova ◽  
V. Demko ◽  
M. Durchan ◽  
K. Mikulova ◽  
...  

2009 ◽  
Vol 425 (2) ◽  
pp. 425-434 ◽  
Author(s):  
Bjoern Gisk ◽  
Yukiko Yasui ◽  
Takayuki Kohchi ◽  
Nicole Frankenberg-Dinkel

HOs (haem oxygenases) catalyse the oxidative cleavage of haem to BV (biliverdin), iron and carbon monoxide. In plants, the product of the reaction is BV IXα, the precursor of the PHY (phytochrome) chromophore and is thus essential for proper photomorphogenesis. Arabidopsis thaliana contains one major biochemically characterized HO (HY1) and three additional putative HOs (HO2, HO3 and HO4). All four proteins are encoded in the nucleus but contain chloroplast translocation sequences at their N-termini. The transit peptides of all four proteins are sufficient for chloroplast translocalization as shown by GFP (green fluorescent protein) reporter gene fusions. Overall, all four proteins can be divided into two subfamilies: HO1 and HO2. Here we show that all members of the HO1 subfamily (HY1, HO3 and HO4) are active monomeric HOs and can convert haem to BV IXα using spinach Fd (ferredoxin) as an electron donor. Addition of a second electron donor, such as ascorbate, led to a 10-fold increase in the haem conversion rate. Furthermore, haem turnover is also promoted by light when spinach thylakoids are present. All HO1 family members displayed similar kinetic parameters indicating they all have a possible involvement in PHY chromophore biosynthesis. HO2 did not yield sufficient amounts of soluble protein and therefore required the construction of a synthetic gene adapted to the codon usage of Escherichia coli. HO2 is unable to bind or degrade haem and therefore it is not a haem oxygenase. However, HO2 shows strong binding of proto IX (protoporphyrin IX), a precursor for both haem and chlorophyll biosynthesis. A possible function of HO2 in the regulation of tetrapyrrole metabolism is discussed.


Genetics ◽  
1995 ◽  
Vol 139 (3) ◽  
pp. 1393-1409 ◽  
Author(s):  
G Roman ◽  
B Lubarsky ◽  
J J Kieber ◽  
M Rothenberg ◽  
J R Ecker

Abstract The response of Arabidopsis thaliana etiolated seedlings to the plant hormone ethylene is a conspicuous phenotype known as the triple response. We have identified genes that are required for ethylene perception and responses by isolating mutants that fail to display a triple response in the presence of exogenous ethylene. Five new complementation groups have been identified. Four of these loci, designated ein4, ein5, ein6 and ein7, are insensitive to ethylene. The fifth complementation group, eir1, is defined by a novel class of mutants that have agravitropic and ethylene-insensitive roots. Double-mutant phenotypes have allowed the positioning of these loci in a genetic pathway for ethylene signal transduction. The ethylene-response pathway is defined by the following loci: ETR1, EIN4, CTR1, EIN2, EIN3, EIN5, EIN6, EIN7, EIR1, AUX1 and HLS1. ctr1-1 is epistatic to etr1-3 and ein4, indicating that CTR1 acts after both ETR1 and EIN4 in the ethylene-response pathway. Mutations at the EIN2, EIN3, EIN5, EIN6 and EIN7 loci are all epistatic to the ctr1 seedling phenotype. The EIR1 and AUX1 loci define a root-specific ethylene response that does not require EIN3 or EIN5 gene activity. HLS1 appears to be required for differential cell growth in the apical hook. The EIR1, AUX1 and HLS1 genes may function in the interactions between ethylene and other plant hormones that occur late in the signaling pathway of this simple gas.


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