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dc.contributor.author
Escandón, Monica
dc.contributor.author
Bigatton, Ezequiel Darío
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dc.contributor.author
Guerrero Sánchez, Victor M.
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dc.contributor.author
Hernández Lao, Tamara
dc.contributor.author
Rey, María Dolores
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dc.contributor.author
Jorrín Novo, Jesús V.
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dc.contributor.author
Castillejo Sánchez, María Ángeles
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dc.date.available
2023-06-26T17:52:19Z
dc.date.issued
2022-06
dc.identifier.citation
Escandón, Monica; Bigatton, Ezequiel Darío; Guerrero Sánchez, Victor M.; Hernández Lao, Tamara; Rey, María Dolores; et al.; Identification of proteases and protease inhibitors in seeds of the recalcitrant forest tree species Quercus ilex; Frontiers Media S.A.; Frontiers in Plant Science; 13; 6-2022; 1-36
dc.identifier.uri
http://hdl.handle.net/11336/201565
dc.description.abstract
Proteases and protease inhibitors have been identified in the recalcitrant species Quercus ilex using in silico and wet methods, with focus on those present in seeds during germination. In silico analyses showed that the Q. ilex transcriptome database contained 2,240 and 97 transcripts annotated as proteases and protease inhibitors, respectively. They belonged to the different families according to MEROPS,1 being the serine and metallo ones the most represented. The data were compared with those previously reported for other Quercus species, including Q. suber, Q. lobata, and Q. robur. Changes in proteases and protease inhibitors alongside seed germination in cotyledon and embryo axis tissues were assessed using proteomics and in vitro and in gel activity assays. Shotgun (LC–MSMS) analysis of embryo axes and cotyledons in nonviable (NV), mature (T1) and germinated (T3) seeds allowed the identification of 177 proteases and 12 protease inhibitors, mostly represented by serine and metallo types. Total protease activity, as determined by in vitro assays using azocasein as substrate, was higher in cotyledons than in embryo axes. There were not differences in activity among cotyledon samples, while embryo axis peaked at germinated T4 stage. Gel assays revealed the presence of protease activities in at least 10 resolved bands, in the Mr range of 60–260 kDa, being some of them common to cotyledons and embryo axes in either nonviable, mature, and germinated seeds. Bands showing quantitative or qualitative changes upon germination were observed in embryo axes but not in cotyledons at Mr values of 60–140 kDa. Proteomics shotgun analysis of the 10 bands with protease activity supported the results obtained in the overall proteome analysis, with 227 proteases and 3 protease inhibitors identified mostly represented by the serine, cysteine, and metallo families. The combined use of shotgun proteomics and protease activity measurements allowed the identification of tissue-specific (e.g., cysteine protease inhibitors in embryo axes of mature acorns) and stage-specific proteins (e.g., those associated with mobilization of storage proteins accumulated in T3 stage). Those proteins showing differences between nonviable and viable seeds could be related to viability, and those variables between mature and germinated could be associated with the germination process. These differences are observed mostly in embryo axes but not in cotyledons. Among them, those implicated in mobilization of reserve proteins, such as the cathepsin H cysteine protease and Clp proteases, and also the large number of subunits of the CNS and 26S proteasome complex differentially identified in embryos of the several stages suggests that protein degradation via CNS/26S plays a major role early in germination. Conversely, aspartic proteases such as nepenthesins were exclusively identified in NV seeds, so their presence could be used as indicator of nonviability.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Frontiers Media S.A.
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights
Atribución-NoComercial-CompartirIgual 2.5 Argentina (CC BY-NC-SA 2.5 AR)
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
GERMINATION
dc.subject
NONORTHODOX SEEDS
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PROTEASE
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PROTEASE ACTIVITY
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PROTEASE INHIBITORS
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PROTEOMICS
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QUERCUS ILEX
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Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Identification of proteases and protease inhibitors in seeds of the recalcitrant forest tree species Quercus ilex
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-06-26T13:40:36Z
dc.identifier.eissn
1664-462X
dc.journal.volume
13
dc.journal.pagination
1-36
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Escandón, Monica. Universidad de Córdoba; España. Universidad de Oviedo; España
dc.description.fil
Fil: Bigatton, Ezequiel Darío. Universidad de Córdoba; España. Universidad Nacional de Córdoba. Facultad de Ciencias Agropecuarias. Departamento de Recursos Naturales. Cátedra de Microbiología Agrícola; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Guerrero Sánchez, Victor M.. Universidad de Oviedo; España. Universidad de Córdoba; España
dc.description.fil
Fil: Hernández Lao, Tamara. Universidad de Córdoba; España
dc.description.fil
Fil: Rey, María Dolores. Universidad de Córdoba; España
dc.description.fil
Fil: Jorrín Novo, Jesús V.. Universidad de Córdoba; España
dc.description.fil
Fil: Castillejo Sánchez, María Ángeles. Universidad de Córdoba; España
dc.journal.title
Frontiers in Plant Science
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fpls.2022.907042
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fpls.2022.907042/full
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