Off-campus UMass Amherst users: To download campus access theses, please use the following link to log into our proxy server with your UMass Amherst user name and password.
Non-UMass Amherst users: Please talk to your librarian about requesting this thesis through interlibrary loan.
Theses that have an embargo placed on them will not be available to anyone until the embargo expires.
Access Type
Campus Access
Document Type
thesis
Degree Program
Molecular & Cellular Biology
Degree Type
Master of Science (M.S.)
Year Degree Awarded
2010
Month Degree Awarded
September
Keywords
Formin homologue, Actin Nucleation, AFH1, AFH5, pollen tube tip growth
Abstract
Dynamic actin remodeling is at the core of a number of fundamental cellular processes in a variety of organisms ranging from animal neuronal outgrowth to pollen tube growth during plant reproduction and asymmetrical cell division in budding yeast. Such dynamism results from a concerted effort of a number of temporally and spatially regulated actin binding proteins. The polymerization and depolymerization of elaborate F-actin networks takes place by the addition and removal of actin subunits at the two filament ends with each end possessing distinct properties, making the filaments themselves polar structures with a fast growing “barbed end” and a slow growing “pointed end”. Although actin polymerization at the barbed end is an efficient and favorable process, the initial filament nucleation step is a much more inefficient and thermodynamically unfavorable process requiring the need for a variety of actin nucleating proteins. These nucleating proteins not only determine the precise location of actin assembly at the cell membrane during polarized cell growth but also directly control the number of force producing filaments. Here we have concentrated our efforts in characterizing a number of Arabidopsis thaliana , Group I membrane bound, formin homologues AFH1, AFH5, AFH6, AFH7, AFH8 and AFH11 using a range of functional genomics tools. Consequently we have shown that AFH5 is a pollen expressed actin nucleating protein localized at the tip of the polarized tube. Genetic alterations of the AFH5 gene using T-DNA gene knockout and gene overexpression both show distinct deformities at the tip of the rapidly growing pollen tube leading to inefficient fertilization during plant reproduction and reduced silique length. In the tip growing root hair cells of Arabidopsis the afh5 mutants show a wavy and bulgy phenotype at the hypocotyl region while the afh1 mutants project branched, split root hairs along the primary root. Although our results do indicate that AFH1 and AFH5 are expressed in the polarized pollen tubes and root hairs their, expression and hence activity is spatially controlled and restricted to different parts of the cell.
DOI
https://doi.org/10.7275/1400872
First Advisor
Alice Y. Cheung