Pedro Carrasco

Dr. Pedro Carrasco

orcid

Research Focus & Metrics

Academic Career Length

44Years (1983-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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11 March 2010 in Planta
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RARuben Alcazar
Ruben Alcazar
Teresa AltabellaTeresa Altabella
Teresa Altabella
FMFrancisco Marco
Francisco Marco
CBCristina Bortolotti
Cristina Bortolotti
MRMatthieu Reymond
Matthieu Reymond
Antonio F. TiburcioAntonio F. Tiburcio
Antonio F. Tiburcio

22 September 2006 in Biotechnology Letters
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Journal Article
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RARuben Alcazar
Ruben Alcazar
FMFrancisco Marco
Francisco Marco
JCJuan C. Cuevas
Juan C. Cuevas
MPMacarena Patron
Macarena Patron
AFAlejandro Ferrando
Alejandro Ferrando
Teresa AltabellaTeresa Altabella
Teresa Altabella

1 January 2011 in Plant Science
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Journal Article
Closed access
RARuben Alcazar
Ruben Alcazar
JCJuan C. Cuevas
Juan C. Cuevas
JPJoan Planas
Joan Planas
XZXavier Zarza
Xavier Zarza
CBCristina Bortolotti
Cristina Bortolotti
Teresa AltabellaTeresa Altabella
Teresa Altabella

8 October 2012 in PLOS ONE
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Journal Article
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BBBorja Belda-Palazón
Borja Belda-Palazón
Leticia RuizLeticia Ruiz
Leticia Ruiz
EMEsmeralda Martí
Esmeralda Martí
STSusana Tárraga
Susana Tárraga
ATAntonio F. Tiburcio
Antonio F. Tiburcio
AFAlejandro Ferrando
Alejandro Ferrando
Plant aminopropyltransferases consist of a group of enzymes that transfer aminopropyl groups derived from decarboxylated S-adenosyl-methionine (dcAdoMet or dcSAM) to propylamine acceptors to produce polyamines, ubiquitous metabolites with positive charge at physiological pH. Spermidine synthase (SPDS) uses putrescine as amino acceptor to form spermidine, whereas spermine synthase (SPMS) and thermospermine synthase (TSPMS) use spermidine as acceptor to synthesize the isomers spermine and thermospermine respectively. In previous work it was shown that both SPDS1 and SPDS2 can physically interact with SPMS although no data concerning the subcellular localization was reported. Here we study the subcellular localization of these enzymes and their protein dimer complexes with gateway-based Bimolecular Fluorescence Complementation (BiFC) binary vectors. In addition, we have characterized the molecular weight of the enzyme complexes by gel filtration chromatography with in vitro assembled recombinant enzymes and with endogenous plant protein extracts. Our data suggest that aminopropyltransferases display a dual subcellular localization both in the cytosol and nuclear enriched fractions, and they assemble preferably as dimers. The BiFC transient expression data suggest that aminopropyltransferase heterodimer complexes take place preferentially inside the nucleus.

1 January 2012 in Plant Science
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Journal Article
Closed access
FEFrancisco J. Escaray
Francisco J. Escaray
AMAna B. Menendez
Ana B. Menendez
AGAndrés Gárriz
Andrés Gárriz
FPFernando L. Pieckenstain
Fernando L. Pieckenstain
MEMaría J. Estrella
María J. Estrella
OROscar A. Ruiz
Oscar A. Ruiz

9 February 2021 in Proceedings of the National Academy of Sciences
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RGRubén González
Rubén González
ABAnamarija Butković
Anamarija Butković
FEFrancisco J. Escaray
Francisco J. Escaray
JMJavier Martínez-Latorre
Javier Martínez-Latorre
ÍMÍzan Melero
Ízan Melero
Santiago F ElenaSantiago F Elena
Santiago F Elena
Environmental conditions are an important factor driving pathogens’ evolution. Here, we explore the effects of drought stress in plant virus evolution. We evolved turnip mosaic potyvirus in well-watered and drought conditions in Arabidopsis thaliana accessions that differ in their response to virus infection. Virus adaptation occurred in all accessions independently of watering status. Drought-evolved viruses conferred a significantly higher drought tolerance to infected plants. By contrast, nonsignificant increases in tolerance were observed in plants infected with viruses evolved under standard watering. The magnitude of this effect was dependent on the plant accessions. Differences in tolerance were correlated to alterations in the expression of host genes, some involved in regulation of the circadian clock, as well as in deep changes in the balance of phytohormones regulating defense and growth signaling pathways. Our results show that viruses can promote host survival in situations of abiotic stress, with the magnitude of such benefit being a selectable trait. Significance Viruses are seen as selfish pathogens that harm their hosts to ensure their own survival. However, metagenomic studies are drawing a new picture in which viruses are present everywhere and not always associated to diseases. A classic observation in plant pathology is that the outcome of infection depends on environmental conditions. Here, using experimental evolution, we show that the relationship between a plant virus and its natural host can evolve from pathogenic to mutualistic under severe drought conditions. While viral strains evolved in normal watering conditions increased their virulence, drought-evolved viral strains confer plants with greater resistance to drought. We show that this transition to mutualism depends on a complex reorganization of hormone-induced signaling pathways and changes in gene expression.