Showing 1 - 10 of 17 Items

Enhancer usage variation assessed via chromatin-conformation within and among three species of Drosophila This record is embargoed.
- Embargo End Date: 2027-05-19
Date: 2022-01-01
Creator: Maia B. Granoski
Access: Embargoed

Determining the influence of proximal Zeste binding sites and promoters on rates of transvection This record is embargoed.
- Embargo End Date: 2026-05-17
Date: 2023-01-01
Creator: Molly Henderson
Access: Embargoed

Identification of MPKs Involved in the Wall Associated Kinase Regulated Stress Response in Arabidopsis thaliana Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2013-05-01
Creator: Patrick J Lariviere
Access: Access restricted to the Bowdoin Community

Investigating the Role of Helicobacter pylori Glycan Biosynthesis in Modulating Host Immune Cell Recognition Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2023-01-01
Creator: Katharine Barrett
Access: Access restricted to the Bowdoin Community

Live imaging of somatic homolog pairing in Drosophila supports a button-based mechanism for pairing facilitated by the genetic insulator gypsy This record is embargoed.
- Embargo End Date: 2026-05-18
Date: 2023-01-01
Creator: Holden D. Hadfield
Access: Embargoed

Cell Adhesion in Arabidopsis thaliana Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2019-05-01
Creator: Natasha Ann Belsky
Access: Access restricted to the Bowdoin Community

The role of the ROG1 protein in pectin perception Access to this record is restricted to members of the Bowdoin community. Log in here to view.
Date: 2014-05-01
Creator: Divya Hoon
Access: Access restricted to the Bowdoin Community
Genetic Analysis of Adhesion Protein ELMO3 in Arabidopsis thaliana
Date: 2022-01-01
Creator: Garrison Asper
Access: Open access
- The Extracellular Matrix (ECM) between plant cells is vital for structure, development, and intercellular adhesion. A pectin rich layer in between cells, the middle lamella, is largely responsible for regulating the adhesive properties of adjacent plant cells. Homogalacturonan (HG) pectin, the most common, is synthesized in the Golgi and secreted into the ECM where it undergoes calcium crosslinking, increasing its adhesive properties. Mutations in proteins essential for HG synthesis can reveal a severe adhesion defective phenotype, where the hypocotyls of dark grown Arabidopsis exhibit cell sloughing, curling, and general disorganization. A family of five ELMO proteins are suspected to act as scaffolds for pectin biosynthesis enzymes. ELMO1 and ELMO4 mutants exhibit an adhesion deficient phenotype, and a double mutant provides evidence of redundancy in function between ELMO1 and ELMO2. ELMO1-GFP co-immunoprecipitated with enzymes required for HG synthesis indicating its role as a scaffold protein. Double mutants of the other ELMO homologues were created to determine if they exhibit functional redundancy, and ELMO1 and ELMO3 appear partially redundant. A gene deletion of ELMO3 was also created using the CRSPR/Cas9 system, resulting in two distinct elmo3 deletion alleles, which were phenotypically identical to the original elmo3-/- mutant. All adhesion defective phenotypes can be partially suppressed by altering the osmoticum and hence turgor that provides pressure on adhesive cells. Lastly, ELMO3-GFP was localized to the Golgi, the site of pectin biosynthesis, further supporting a common role of the ELMOs in pectin biosynthesis.

Role of Polycomb group proteins in regulation of eyes absent gene expression in Drosophila melanogaster This record is embargoed.
- Embargo End Date: 2027-05-16
Date: 2024-01-01
Creator: Joanne Du
Access: Embargoed
Examining the role of GRP and LIK1 in Wall Associated Kinase (WAK) perception of pectin in the plant cell wall
Date: 2017-01-01
Creator: Jack Ryan Mitchell
Access: Open access
- Wall associated kinases (WAKs) are cell membrane bound receptor kinases that bind pectin and pectin fragments (OGs).The binding of WAKs to pectin sends a growth signal required for cell elongation and plant development. WAKs bind OGs with higher affinity than native pectin and instead activate a stress response. Glycine rich proteins (GRPs) are secreted cell wall proteins of unknown function. Seven GRPs with 65% sequence similarity are coded on a 90kb locus of Arabidopsis chromosome 2. GRP3 and WAK1 have been shown to bind in vitro, but single null mutations have no discernible phenotype, suggesting that the GRPs are redundant. Low recombination frequency has made multiple mutations difficult to achieve, but in this thesis, CRISPR/Cas9 technology was used to induce deletions of the GRP locus. The promoters pYAO and pICU2 drove Cas9 expression in transformed Arabidopsis plants. The presence of a deletion and Cas9 were detected by PCR. While somatic mutations were induced, there was no inheritance of the GRP deletion, indicating that pYAO and pICU2 do not drive Cas9 to induce deletions in progenitor cells. LIK1 is a CERK1 interacting kinase implicated in mediating response to various microbe associated molecular patterns (MAMP) such as chitin, flagellin, and peptidoglycans. LIK1 exhibits a drastic increase in phosphorylation in response to OG treatment, making it a candidate for a co-receptor to WAK. T-DNA insertions to the 5’UTR of LIK1 were used to examine the effect of a lik1 mutation on the OG induced stress response. lik1/lik1 mutant seedlings were grown in the presence and absence of OGs, and RNA was isolated. qPCR was used on cDNA to examine FADLOX expression, a reporter for the transcriptional response to OGs. The lik1/lik1 mutant caused a reduction in the OG induced transcriptional response. However, increased LIK1 expression was associated with the T-DNA insertion indicating that LIK1 inhibits the WAK stress response pathway. Understanding the roles of GRP and LIK1 in moderating WAK mediated pathogenic response in Arabidopsis will enable a better understanding of plant resistance to pathogen invasion in the greater plant kingdom.