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dc.contributor.advisorMoore, D. Blaine, 1972-
dc.contributor.advisorBarkman, Todd
dc.contributor.authorColebrook, Kate
dc.date.accessioned2019-04-06T15:40:38Z
dc.date.available2019-04-06T15:40:38Z
dc.date.issued2019
dc.identifier.urihttp://hdl.handle.net/10920/36752
dc.descriptionv, 39 p.en_US
dc.description.abstractSalicylic acid carboxyl methyltransferase (SAMT) and benzoic acid carboxyl methyltransferase (BAMT) are enzymes in plants which catalyze the methylation of small carboxylate containing molecules: salicylic acid (SA) and benzoic acid (BA). Both of these small molecules function in various essential plant pathways. These pathways aid in critical functions, such as plant defense against abiotic and biotic stressors, and in pollinator attraction. The evolution of SAMT from BAMT was positively selected for to increase the specificity and control of crucial pathways. The functionality of SAMT has been maintained across studied descendant families of dicots. RNA extracted from Daucus carota subsp. Sativus, Ipomea alba, Viola mandshurica, and Punica granatum was used in enzyme functional assays in order to determine SAMT substrate preference. The SAMT enzymes in these previously unstudied families were all found to prefer SA over BA despite variation in the active site. This preference matches those of the SAMT enzymes in other experimentally-determined dicots. The maintenance of the SAMT gene and substrate preference of SA over BA across families of dicots suggests that SAMT does not lower organism fitness. This suggests that the increased specialization of enzymes for SA and BA methylation is advantageous in plant fitness. Understanding how best to aid plant fitness may provide insights in how best to protect produce naturally and effectively.en_US
dc.format.mimetypeapplication/pdf
dc.language.isoen_USen_US
dc.publisherKalamazoo Collegeen_US
dc.relation.ispartofKalamazoo College Biology Senior Individualized Projects Collection
dc.rightsU.S. copyright laws protect this material. Commercial use or distribution of this material is not permitted without prior written permission of the copyright holder.
dc.titleSubstrate Preference and Function of Salicylic Acid Methyltransferase in Dicotsen_US
dc.typeThesisen_US
KCollege.Access.ContactIf you are not a current Kalamazoo College student, faculty, or staff member, email dspace@kzoo.edu to request access to this thesis.


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    This collection includes Senior Individualized Projects (SIP's) completed in the Biology Department. Abstracts are generally available to the public, but PDF files are available only to current Kalamazoo College students, faculty, and staff.

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