scholarly journals A Rice Phytochrome A in Arabidopsis: The Role of the N-terminus under red and far-red light

2008 ◽  
Vol 1 (1) ◽  
pp. 84-102 ◽  
Author(s):  
Julia Kneissl ◽  
Tomoko Shinomura ◽  
Masaki Furuya ◽  
Cordelia Bolle
Keyword(s):  
Red Light ◽  
Phytochrome A ◽  
N Terminus

The role of phytochrome C in gravitropism and phototropism in Arabidopsis thaliana

2008 ◽  
Vol 35 (4) ◽  
pp. 298 ◽  
Author(s):  
Prem Kumar ◽  
Crystal E. Montgomery ◽  
John Z. Kiss
Keyword(s):  
Arabidopsis Thaliana ◽  
Blue Light ◽  
Leaf Morphology ◽  
Red Light ◽  
Phytochrome A ◽  
Inflorescence Stems ◽  
Root Gravitropism ◽  
Positive Effect ◽  
Rosette Leaf

The phytochrome (phy) photoreceptors, which consist of a small gene family PHYA-E in dicot plants, play important roles in regulating many light-induced responses in plants. Although the best characterised phytochromes are phytochrome A (phyA) and phytochrome (phyB), the functions of phyD and phyE have been increasingly studied. Phytochrome C (phy C) has been the most poorly understood member of the photoreceptor family, since isolation of phyC mutants only has been accomplished within the last few years. Recent reports show that phyC functions in hypocotyl elongation, rosette leaf morphology, and timing of flowering. In the present study, we show that phyC plays a role in tropisms in seedlings and inflorescence stems of light-grown Arabidopsis thaliana (L.) Heynh. (Wassilewskija ecotype). Phytochrome C has a positive effect on gravitropism in hypocotyls and stems, but it has a limited role in root gravitropism. In contrast, phyC attenuates the positive phototropic response to blue light in hypocotyls and the red-light-based positive phototropism in roots. Phytochrome D (phy D) also mediates gravitropism in hypocotyls and inflorescence stems and attenuates positive phototropism in response to blue in hypocotyls and stems. Thus, phyC can be added to the list of the other four phytochromes, which play various roles in both gravitropism and phototropism in plant organs. This report also supports the growing body of evidence demonstrating cross talk between phytochromes and blue-light photoreceptors.

scholarly journals Hinge region of Arabidopsis phyA plays an important role in regulating phyA function

2018 ◽  
Vol 115 (50) ◽  
pp. E11864-E11873 ◽  
Author(s):  
Yangyang Zhou ◽  
Li Yang ◽  
Jie Duan ◽  
Jinkui Cheng ◽  
Yunping Shen ◽  
...  
Keyword(s):  
Light Exposure ◽  
Red Light ◽  
Light Response ◽  
Hinge Region ◽  
Phytochrome A ◽  
Serine Residue ◽  
Signal Transducers ◽  
And Function

Phytochrome A (phyA) is the only plant photoreceptor that perceives far-red light and then mediates various responses to this signal. Phosphorylation and dephosphorylation of oat phyA have been extensively studied, and it was shown that phosphorylation of a serine residue in the hinge region of oat phyA could regulate the interaction of phyA with its signal transducers. However, little is known about the role of the hinge region of Arabidopsis phyA. Here, we report that three sites in the hinge region of Arabidopsis phyA (i.e., S590, T593, and S602) are essential in regulating phyA function. Mutating all three of these sites to either alanines or aspartic acids impaired phyA function, changed the interactions of mutant phyA with FHY1 and FHL, and delayed the degradation of mutant phyA upon light exposure. Moreover, the in vivo formation of a phosphorylated phyA form was greatly affected by these mutations, while our data indicated that the abundance of this phosphorylated phyA form correlated well with the extent of phyA function, thus suggesting a pivotal role of the phosphorylated phyA in inducing the far-red light response. Taking these data together, our study reveals the important role of the hinge region of Arabidopsis phyA in regulating phyA phosphorylation and function, thus linking specific residues in the hinge region to the regulatory mechanisms of phyA phosphorylation.

The role of SERT N-terminus in amphetamine-induced efflux

2016 ◽  
Vol 4 (Suppl. 3) ◽  
pp. A4.17
Author(s):  
Fatma Aslı Erdem
Keyword(s):  
N Terminus

scholarly journals RNA Helicase A Regulates the Replication of RNA Viruses

Viruses ◽  
2021 ◽  
Vol 13 (3) ◽  
pp. 361
Author(s):  
Rui-Zhu Shi ◽  
Yuan-Qing Pan ◽  
Li Xing
Keyword(s):  
Virus Replication ◽  
Rna Binding ◽  
Rna Viruses ◽  
Rna Helicase ◽  
Rna Helicase A ◽  
Double Stranded Rna ◽  
Binding Domains ◽  
N Terminus

The RNA helicase A (RHA) is a member of DExH-box helicases and characterized by two double-stranded RNA binding domains at the N-terminus. RHA unwinds double-stranded RNA in vitro and is involved in RNA metabolisms in the cell. RHA is also hijacked by a variety of RNA viruses to facilitate virus replication. Herein, this review will provide an overview of the role of RHA in the replication of RNA viruses.

scholarly journals Chimeric elk/mouse prion proteins in transgenic mice

2013 ◽  
Vol 94 (2) ◽  
pp. 443-452 ◽  
Author(s):  
Gültekin Tamgüney ◽  
Kurt Giles ◽  
Abby Oehler ◽  
Natrina L. Johnson ◽  
Stephen J. DeArmond ◽  
...  
Keyword(s):  
Neurodegenerative Disorder ◽  
Prion Proteins ◽  
Second Line ◽  
Mouse Line ◽  
Wasting Disease ◽  
C Terminus ◽  
Incubation Periods ◽  
N Terminus ◽  
Mouse Lines

Chronic wasting disease (CWD) of deer and elk is a highly communicable neurodegenerative disorder caused by prions. Investigations of CWD are hampered by slow bioassays in transgenic (Tg) mice. Towards the development of Tg mice that will be more susceptible to CWD prions, we created a series of chimeric elk/mouse transgenes that encode the N terminus of elk PrP (ElkPrP) up to residue Y168 and the C terminus of mouse PrP (MoPrP) beyond residue 169 (mouse numbering), designated Elk3M(SNIVVK). Between codons 169 and 219, six residues distinguish ElkPrP from MoPrP: N169S, T173N, V183I, I202V, I214V and R219K. Using chimeric elk/mouse PrP constructs, we generated 12 Tg mouse lines and determined incubation times after intracerebral inoculation with the mouse-passaged RML scrapie or Elk1P CWD prions. Unexpectedly, one Tg mouse line expressing Elk3M(SNIVVK) exhibited incubation times of <70 days when inoculated with RML prions; a second line had incubation times of <90 days. In contrast, mice expressing full-length ElkPrP had incubation periods of >250 days for RML prions. Tg(Elk3M,SNIVVK) mice were less susceptible to CWD prions than Tg(ElkPrP) mice. Changing three C-terminal mouse residues (202, 214 and 219) to those of elk doubled the incubation time for mouse RML prions and rendered the mice resistant to Elk1P CWD prions. Mutating an additional two residues from mouse to elk at codons 169 and 173 increased the incubation times for mouse prions to >300 days, but made the mice susceptible to CWD prions. Our findings highlight the role of C-terminal residues in PrP that control the susceptibility and replication of prions.

Far-Red Light Blocks Greening of Arabidopsis Seedlings via a Phytochrome A: Mediated Change in Plastid Development

1996 ◽  
Vol 8 (4) ◽  
pp. 601 ◽  
Author(s):  
Simon A. Barnes ◽  
Naoko K. Nishizawa ◽  
Ronaldo B. Quaggio ◽  
Garry C. Whitelam ◽  
Nam-Hai Chua
Keyword(s):  
Red Light ◽  
Phytochrome A ◽  
Plastid Development

Two native types of phytochrome A, phyAʹ and phyAʺ, differ by the state of phosphorylation at the N-terminus as revealed by fluorescence investigations of the Ser/Ala mutant of rice phyA expressed in transgenic Arabidopsis

2018 ◽  
Vol 45 (2) ◽  
pp. 150 ◽  
Author(s):  
Vitaly A. Sineshchekov ◽  
Larissa A. Koppel ◽  
Cordelia Bolle
Keyword(s):  
Transgenic Arabidopsis ◽  
Emission Spectra ◽  
Total Content ◽  
The State ◽  
Serine Phosphorylation ◽  
Phytochrome A ◽  
Wild Type ◽  
Etiolated Seedlings ◽  
Pre Treatment

Phytochrome A (phyA) mediates different photoresponses what may be connected with the existence of its two types, phyAʹ and phyAʹʹ, differing by spectroscopic, photochemical and functional properties. We investigated a role of phyA phosphorylation in their formation turning to transgenic Arabidopsis thaliana (L. Heynh.) phyA or phyAphyB mutants overexpressing rice wild-type phyA (phyA WT) or mutant phyA (phyA SA) with the first 10 serines substituted by alanines. This prevents phyA phosphorylation at these sites and modifies photoresponses. Etiolated seedlings were employed and phyA parameters were evaluated with the use of low temperature fluorescence spectroscopy and photochemistry. Germination of seeds was induced by white light (WL) pre-treatment for 15 min or 3 h. Emission spectra of rice phyA WT and phyA SA were similar and their total content was comparable. However, the phyAʹ/phyAʹʹ proportion in phyA WT was high and varied with the duration of the WL pre-treatment, whereas in phyA SA it was substantially shifted towards phyAʹʹ and did not depend on the pre-illumination. This suggests that phyA SA comprises primarily or exclusively the phyAʹʹ pool and supports the notion that the two phyA types differ by the state of serine phosphorylation. phyAʹʹ was also found to be much more effective in the germination induction than phyAʹ.

scholarly journals Role of the N-terminus in the structure and stability of chicken annexin V

FEBS Letters ◽  
1997 ◽  
Vol 416 (2) ◽  
pp. 217-220 ◽  
Author(s):  
David Arboledas ◽  
Nieves Olmo ◽  
Mª Antonia Lizarbe ◽  
Javier Turnay
Keyword(s):  
Annexin V ◽  
Structure And Stability ◽  
N Terminus

scholarly journals Epitope mapping of human respiratory syncytial virus 22K transcription antitermination factor: role of N-terminal sequences in protein folding

2005 ◽  
Vol 86 (4) ◽  
pp. 1103-1107 ◽  
Author(s):  
Blanca García-Barreno ◽  
John Steel ◽  
Monica Payá ◽  
Luis Martínez-Sobrido ◽  
Teresa Delgado ◽  
...  
Keyword(s):  
Protein Folding ◽  
Respiratory Syncytial Virus ◽  
Western Blotting ◽  
Epitope Mapping ◽  
Human Respiratory Syncytial Virus ◽  
N Terminus ◽  
Transcription Antitermination ◽  
Syncytial Virus ◽  
Antibody Epitopes

The reactivity of a panel of 12 monoclonal antibodies raised against the human respiratory syncytial virus 22 kDa (22K) protein was tested by Western blotting with a set of 22K deletion mutants. The results obtained identified sequences in the C-terminal half of the 22K polypeptide required for integrity of most antibody epitopes, except for epitope 112, which was lost in mutants with short N-terminal deletions. This antibody, in contrast to the others, failed to immunoprecipitate the native 22K protein, indicating that the N terminus of this protein is buried in the native molecule and exposed only under the denaturing conditions of Western blotting. In addition, N-terminal deletions that abolished reactivity with monoclonal antibody 112 also inhibited phosphorylation of the 22K protein previously identified at Ser-58 and Ser-61, suggesting that the N terminus is important in regulating the 22K protein phosphorylation status, most likely as a result of its requirement for protein folding.

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