Theses and Dissertations at Montana State University (MSU)
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Item Indirect selection for grain protein in winter wheat(Montana State University - Bozeman, College of Agriculture, 1988) Noaman, Maher Noaman MohamedItem Serological studies of moth proteins with special reference to specific immune bodies and their phylogenetic significance(Montana State University - Bozeman, College of Agriculture, 1933) Martin, SaxonItem The relationship of Gliadin and glutenin subunits to breadmaking characteristics in winter wheat(Montana State University - Bozeman, College of Agriculture, 1988) Al-Khawlani, Mohamed AliItem Yield and yield components of sainfoin (Onobrychis viciaefolia Scop.) seed and an evaluation of its use as a protein supplement(Montana State University - Bozeman, College of Agriculture, 1973) Ditterline, R. L.Item A serological comparison of potato virus X protein prior and subsequent to partial enzymatic hydrolysis(Montana State University - Bozeman, College of Agriculture, 1971) Secor, Gary AllenItem Analysis of nitrogen reallocation from senescing barley leaves : characterization of the influence of a high-grain protein content locus on chromosome six, and molecular cloning and heterologous expression of a serine carboxypeptidase(Montana State University - Bozeman, College of Agriculture, 2008) Heidlebaugh, Nancy Marie; Chairperson, Graduate Committee: Andreas M. Fisher.In cereals, senescence is a highly regulated and organized process in which the nutrients located in the leaves are translocated to the developing seeds. During this process multiple signaling cascades are activated either up-regulating or down-regulating senescence related genes. The majority of the nitrogen to be remobilized is located in the leaves in plastidial proteins, especially Rubisco. These proteins must be degraded before their components can be translocated to be reutilized in the seeds. The mechanism for plastidial protein degradation is largely unknown at this time. Proteases located in lytic vacuolar compartments, including carboxypeptidases, have been found to be up-regulated during senescence, which may indicate their involvement in the degradation of plastidial proteins. In a recent genomic study a serine carboxypeptidase, cp-mIII, was found to be up-regulated in senescing leaves. Further characterization and localization of this protease could lead to an increased understanding of the mechanisms of protein degradation within the leaves during senescence. After the proteins are degraded they are transported to the developing seeds to be reincorporated into grain storage proteins.