Luis Gomez

Dr. Luis Gomez

Centre for Plant Biotechnology and Genomics (CBGP UPM-INIA), Campus de Montegancedo, Universidad Politécnica de Madrid, 28223 Madrid, Spain
orcid

Research Focus & Metrics

Academic Career Length

41Years (1986-Present)

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

Representative Publications

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1 June 2020 in Plants
Verified
Journal Article
Open access
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GCGerardo Carrera-Castaño
Gerardo Carrera-Castaño
JCJulián Calleja-Cabrera
Julián Calleja-Cabrera
MPMonica Pernas
Monica Pernas
Luis GomezLuis Gomez
Luis Gomez
Luis  Oñate-Sánchez Luis Oñate-Sánchez
Luis Oñate-Sánchez
The ability of a seed to germinate and establish a plant at the right time of year is of vital importance from an ecological and economical point of view. Due to the fragility of these early growth stages, their swiftness and robustness will impact later developmental stages and crop yield. These traits are modulated by a continuous interaction between the genetic makeup of the plant and the environment from seed production to germination stages. In this review, we have summarized the established knowledge on the control of seed germination from a molecular and a genetic perspective. This serves as a “backbone” to integrate the latest developments in the field. These include the link of germination to events occurring in the mother plant influenced by the environment, the impact of changes in the chromatin landscape, the discovery of new players and new insights related to well-known master regulators. Finally, results from recent studies on hormone transport, signaling, and biophysical and mechanical tissue properties are underscoring the relevance of tissue-specific regulation and the interplay of signals in this crucial developmental process.

1 June 1996 in Glycobiology
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Journal Article
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GGGloria Garcia-Casado
Gloria Garcia-Casado
RSRosa Sanchez-Monge
Rosa Sanchez-Monge
MCMaarten J. Chrispeels
Maarten J. Chrispeels
Alicia ArmentiaAlicia Armentia
Alicia Armentia
GSGabriel Salcedo
Gabriel Salcedo
Luis GomezLuis Gomez
Luis Gomez
Many plant proteins, particularly those found in foods and pollen, are known to act as sensitizing agents in humans upon repeated exposure. Among the cereal flour proteins involved in asthmatic reactions, those members of the α-amylase inhibitor family which are glycosylated, polypeptides BMAI-1, BTAI-CMb*, and WTAI-CM16* are particularly reactive both in vivo and in vitro. We show here that these major glycoprotein allergens carry a single asparagine-linked complex glycan that contains both β1←2 xylose and α1←3 fucose. Evidence is presented that the xylosyl residue and, to a lesser extent, the fucosyl residue are key IgE-binding epitopes and largely responsible for the allergenicity of these and unrelated proteins from plants and insects. Our results suggest that the involvement of xylose- and fucose-containing complex glycans in allergenic responses may have been underestimated previously; these glycans provide a structural basis to help explain the cross-reactivities often observed between pollen, vegetable food, and insect allergens.

28 April 2005 in Proceedings of the National Academy of Sciences
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Journal Article
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ARAlberto Ramos
Alberto Ramos
EPEstefanía Pérez-Solís
Estefanía Pérez-Solís
CICristian Ibáñez
Cristian Ibáñez
RCRosa Casado
Rosa Casado
CCCarmen Collada
Carmen Collada
IAIsabel Allona
Isabel Allona
Circadian clock performance during winter dormancy has been investigated in chestnut by using as marker genesCsTOC1andCsLHY, which are homologous to essential components of the central circadian oscillator inArabidopsis. During vegetative growth, mRNA levels of these two genes in chestnut seedlings and adult plants cycled daily, as expected. However, during winter dormancy,CsTOC1andCsLHYmRNA levels were high and did not oscillate, indicating that the circadian clock was altered. A similar disruption was induced by chilling chestnut seedlings (to 4°C). Normal cycling resumed when endodormant or cold-treated plants were returned to 22°C. The behavior ofCsTOC1andCsLHYduring a cold response reveals a relevant aspect of clock regulation not yet encountered inArabidopsis.

15 January 1992 in Biochemical Journal
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Journal Article
Closed access
RSR Sanchez-Monge
R Sanchez-Monge
Luis GomezLuis Gomez
Luis Gomez
DBD Barber
D Barber
CLC Lopez-Otin
C Lopez-Otin
AAA Armentia
A Armentia
GSG Salcedo
G Salcedo
A 16 kDa protein, designated CM16*, which strongly binds IgE from baker's-asthma patients has been identified as a glycosylated form of the previously reported WTAI-CM16, which is a subunit of the wheat tetrameric alpha-amylase inhibitor. A glycosylated form (CMb*) of BTAI-CMb, the equivalent inhibitor subunit from barley, has been also found to have significantly enhanced IgE-binding capacity. In all, 14 purified members of the alpha-amylase/trypsin-inhibitor family showed very different IgE-binding capacities when tested by a dot-blot assay. The glycosylated components CM16*, CMb* and the previously described non-glycosylated 14.5 kDa allergen from barley (renamed BMAI-1) were found to be the strongest allergens.

1 June 1999 in Plant Physiology
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Journal Article
Closed access
ÁSÁlvaro Soto
Álvaro Soto
IAIsabel Allona
Isabel Allona
CCCarmen Collada
Carmen Collada
MGMaría Ángeles Guevara
María Ángeles Guevara
RCRosa Casado
Rosa Casado
Luis GomezLuis Gomez
Luis Gomez
A small heat-shock protein (sHSP) that shows molecular chaperone activity in vitro was recently purified from mature chestnut (Castanea sativa) cotyledons. This protein, renamed here as CsHSP17.5, belongs to cytosolic class I, as revealed by cDNA sequencing and immunoelectron microscopy. Recombinant CsHSP17.5 was overexpressed in Escherichia coli to study its possible function under stress conditions. Upon transfer from 37°C to 50°C, a temperature known to cause cell autolysis, those cells that accumulated CsHSP17.5 showed improved viability compared with control cultures. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of cell lysates suggested that such a protective effect in vivo is due to the ability of recombinant sHSP to maintain soluble cytosolic proteins in their native conformation, with little substrate specificity. To test the recent hypothesis that sHSPs may be involved in protection against cold stress, we also studied the viability of recombinant cells at 4°C. Unlike the major heat-induced chaperone, GroEL/ES, the chestnut sHSP significantly enhanced cell survivability at this temperature. CsHSP17.5 thus represents an example of a HSP capable of protecting cells against both thermal extremes. Consistent with these findings, high-level induction of homologous transcripts was observed in vegetative tissues of chestnut plantlets exposed to either type of thermal stress but not salt stress.

1 January 2019 in Molecular Plant
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Journal Article
Open access
RSRocío Sánchez-Montesino
Rocío Sánchez-Montesino
LBLaura Bouza-Morcillo
Laura Bouza-Morcillo
JMJulietta Marquez
Julietta Marquez
MGMelania Ghita
Melania Ghita
SDSalva Duran-Nebreda
Salva Duran-Nebreda
Luis  Oñate-Sánchez Luis Oñate-Sánchez
Luis Oñate-Sánchez
A key component of seed germination is the interplay of mechanical forces governing embryo growth and the surrounding restraining endosperm tissue. Endosperm cell separation is therefore thought to play a critical role in the control of this developmental transition. Here we demonstrate that in Arabidopsis thaliana seeds, endosperm cell expansion is a key component of germination. Endosperm cells expand to accommodate embryo growth prior to germination. We show that this is an actively regulated process supported by spatiotemporal control of the cell expansion gene EXPANSIN 2 (EXPA2). The NAC transcription factors NAC25 and NAC1L were identified as upstream regulators of EXPA2 expression, gibberellin-mediated endosperm expansion, and seed germination. The DELLA protein RGL2 repressed activation of the EXPA2 promoter by NAC25/NAC1L. Taken together, our findings uncover a key role of the GA/DELLA-NAC25/NAC1L-EXPA2 network in regulating endosperm cell expansion to control the seed-to-seedling transition.