Showing 1 - 10 of 14 Items

- Restriction End Date: 2025-06-01
Date: 2020-01-01
Creator: Boris S. Dimitrov
Access: Access restricted to the Bowdoin Community

- Restriction End Date: 2026-06-01
Date: 2021-01-01
Creator: Kodie R Garza
Access: Access restricted to the Bowdoin Community

- Embargo End Date: 2027-05-15
Date: 2024-01-01
Creator: Victoria Dunphy
Access: Embargoed
Date: 2021-01-01
Creator: Andrew Close Bolender
Access: Open access
- Plant cell adhesion is mediated by the extracellular matrix (ECM) or cell wall and plays an important role in plant morphogenesis and development. The amount, modification, and cleavage of pectin in the cell wall are major contributors to the adhesive properties of the ECM. To gain a more complete picture of plant cell adhesion processes, Arabidopsis thaliana seedlings were previously mutagenized and screened for hypocotyl adhesion defects. Genomic sequencing of one plant exhibiting an adhesion defect, isolate 242, showed that two mutations, one in cellulose synthase (CesA1) and another in a sugar transporter, are candidates for the causative mutation. This thesis reports that CesA1 is necessary for proper plant cell adhesion, while the sugar transporter encoded at At4g32390 is not. Dark grown seedlings homozygous for mutations in CesA1 stain in ruthenium red, indicating atypical adhesion, while those homozygous for null mutations in At4g32390 do not. Previous study of another adhesion mutant revealed ELMO1, a Golgi protein necessary for plant cell adhesion, and four additional homologs ELMO2-5 in the A. thaliana genome. Two of these homologs, ELMO2 and ELMO3, fused to GFP, colocalized with mCherry-MEM1 markers in the Golgi, but not mCherry-NLM12 ER markers, indicating that ELMO2 and ELMO3 are also Golgi proteins.

Date: 2014-05-01
Creator: Nicholas J Saba
Access: Access restricted to the Bowdoin Community

- Embargo End Date: 2027-05-19
Date: 2022-01-01
Creator: Serena Jonas
Access: Embargoed

- Restriction End Date: 2025-06-01
Date: 2020-01-01
Creator: Diego Andres Villamarin
Access: Access restricted to the Bowdoin Community

- Embargo End Date: 2026-05-18
Date: 2023-01-01
Creator: Holden D. Hadfield
Access: Embargoed
Date: 2024-01-01
Creator: Jared Lynch
Access: Open access
- The mitochondrial genome has historically been relegated to a neutral genetic marker, but new evidence suggests mitochondrial DNA to be a target for adaptation to environmental stress. The invasive European green crab (Carcinus maenas) exemplifies this in the Gulf of Maine’s hybrid zone, where interbreeding populations exhibit thermal tolerances influenced by mitochondrial genotype. To better understand the mechanism behind this phenomenon, the effect of mitochondrial genotype on mitochondrial activity was tested by measuring mtDNA copy number (mtCN) and the activity of complex I, II, and IV of the electron transport system via high-resolution respirometry. Mitochondria isolated from frozen heart tissue were measured at three temperature points—5°C, 25°C, and 37°C—to represent thermal stresses and a control. It was predicted that cold-adapted haplogroups would exhibit both higher mtCN and increased activity for each complex, either across all temperatures or exclusively at 5°C compared to a warm-adapted haplogroup. Initial comparisons of mitochondria from fresh and frozen tissue at 25°C found lower activity for complex II and IV in frozen extracts, but they continued to be used for convenience. No differences were observed across haplogroups for mtCN or high-resolution respirometry, suggesting that mitochondrial activity does not underlie differences in thermal tolerance. However, temperature greatly influenced activity measurements with complex II and IV exhibiting the highest rates at 37°C while complex I exhibited optimal activity at 25°C. This study represents the first of its kind for C. maenas, providing a foundation for future experiments to continue exploring mitochondria in the context of adaptive evolution.

Date: 2019-05-01
Creator: Natasha Ann Belsky
Access: Access restricted to the Bowdoin Community