Presentation Title
The C-terminal Headpiece Domain of Plant Villin 4 Demonstrates a Distinct Surface Charge Distribution Pattern and Low-affinity Specific Binding for F-actin
Presentation Type
Poster
Abstract
The Villin family of proteins are F-actin regulators, which play key roles in cytoskeleton organization and regulation in plants and vertebrates. One of these members, villin 4, is found in root hairs of plants, which are single cell extensions off the main root responsible for the uptake of water and nutrients. It was shown in A.thaliana that contained a mutated version of villin 4 had shorter and sparser root hairs, which led to a weaker capacity to absorb water compared to wild type plants. Our lab is currently investigating the roll of villin 4, specifically by identifying the actin binding sites as well as the structure of its domains. My thesis project specifically investigated the headpiece domain on villin 4, a domain in the villin family generally known to have actin binding capability The research presented here is the solution structure of the villin 4 headpiece domain which has low-affinity specific binding for F-actin.
Start Date
6-5-2017 12:15 PM
End Date
6-5-2017 2:00 PM
Genre/Form
posters
Subjects - Topical (LCSH)
Plants--Abnormalities; Plants--Absorption of water; Proteins--Research
Type
Event
Format
application/pdf
Language
English
The C-terminal Headpiece Domain of Plant Villin 4 Demonstrates a Distinct Surface Charge Distribution Pattern and Low-affinity Specific Binding for F-actin
Miller Hall
The Villin family of proteins are F-actin regulators, which play key roles in cytoskeleton organization and regulation in plants and vertebrates. One of these members, villin 4, is found in root hairs of plants, which are single cell extensions off the main root responsible for the uptake of water and nutrients. It was shown in A.thaliana that contained a mutated version of villin 4 had shorter and sparser root hairs, which led to a weaker capacity to absorb water compared to wild type plants. Our lab is currently investigating the roll of villin 4, specifically by identifying the actin binding sites as well as the structure of its domains. My thesis project specifically investigated the headpiece domain on villin 4, a domain in the villin family generally known to have actin binding capability The research presented here is the solution structure of the villin 4 headpiece domain which has low-affinity specific binding for F-actin.