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Study of bioactive proteins in the roots and root exudates of model plants

dc.contributor.authorDe-la-Peña, Clelia, author
dc.contributor.authorVivanco, Jorge M., advisor
dc.date.accessioned2024-03-13T19:26:11Z
dc.date.available2024-03-13T19:26:11Z
dc.date.issued2007
dc.description.abstractThe plant root system serves many roles, including anchorage and uptake of nutrients and water. The ability of roots to release a wide range of organic and inorganic compounds into the rhizosphere to communicate with roots of other plants and other organisms has been the focus of recent studies. Among the compounds released into the rhizosphere, proteins comprise an important amount of energy secreted by roots but have not been studied in detail. In the present study, I conducted a proteomic and enzymatic analysis of Arabidopsis thaliana root exudation across a developmental gradient to track the changes that occur in the root-secreted proteins at different plant developmental stages. Further, I found that the secretion of proteins (including pathogenesis-related [PR] proteins, myrosinases, and enzymes related to protein refolding) was qualitatively and quantitatively related to the growth stage of the plant. For instance, the intensity and activity of PR proteins such as chitinases were higher at peak flowering times than at any other time during Arabidopsis development. I also studied the root secretion of proteins by two model plants (Medicago sativa and A. thaliana) during their interaction with the symbiont of one of these specks (Sinorhizobium meliloti) and with an opportunistic pathogen of A. thaliana (Pseudomonas syringae pv. tomato DC3000). I found that the early interactions between M.sativa and S. meliloti induced exudation of enzymes such as acid chitinases, thaumatin proteins, PR10 and PR1 proteins. However, these proteins were not induced when M. saliva was inoculated with P. syringae DC3000. In addition, I found that P. syringae DC3000 could differentially induce the secretion of proteins related to defense in A. thaliana, whereas S. meliloti did not provoke the same response. The final study of my dissertation focused on the activity of ribosome-inactivating proteins (RIPS, PC 3.2.2.22) in Arabidopsis thaliana. Based on amino acid sequencing, it was determined that the purified RIP had homology to the mature form of a pectin methylesterase (PME, At1g11580); this purified protein showed PME activity. Further the A. thaliana full-length and mature PMF forms were cloned into the expression vector PQE30 and both constructs were expressed in Escherichia coli.
dc.format.mediumborn digital
dc.format.mediumdoctoral dissertations
dc.identifierETDF_De-la-Peña_2007_3299757.pdf
dc.identifier.urihttps://hdl.handle.net/10217/237675
dc.languageEnglish
dc.language.isoeng
dc.publisherColorado State University. Libraries
dc.relation.ispartof2000-2019
dc.rightsCopyright and other restrictions may apply. User is responsible for compliance with all applicable laws. For information about copyright law, please see https://libguides.colostate.edu/copyright.
dc.rights.licensePer the terms of a contractual agreement, all use of this item is limited to the non-commercial use of Colorado State University and its authorized users.
dc.subjectbioactive proteins
dc.subjectplant-microbe interaction
dc.subjectroot exudates
dc.subjectroots
dc.subjecthorticulture
dc.subjectplant sciences
dc.titleStudy of bioactive proteins in the roots and root exudates of model plants
dc.typeText
dcterms.rights.dplaThis Item is protected by copyright and/or related rights (https://rightsstatements.org/vocab/InC/1.0/). You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s).
thesis.degree.disciplineHorticulture and Landscape Architecture
thesis.degree.grantorColorado State University
thesis.degree.levelDoctoral
thesis.degree.nameDoctor of Philosophy (Ph.D.)

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