Investigating Small Heat Shock Protein Function in Plants

Presenter

Haofeng Lin

Campus

UMass Amherst

Sponsor

Elizabeth Vierling, Department of Biochemistry and Molecular Biology, UMass Amherst

Schedule

Session 1, 10:30 AM - 11:15 AM [Schedule by Time][Poster Grid for Time/Location]

Location

Poster Board A63, Campus Center Auditorium, Row 4 (A61-A80) [Poster Location Map]

Abstract

We are investigating the function of cytosolic small heat shock proteins (sHSPs)  and their role in stress tolerance and normal development in plants. sHSPs are ATP-independent molecular chaperones that are proposed to bind denaturing proteins to prevent their irreversible aggregation. These proteins are highly expressed when plants experience elevated temperatures, as well as during specific stages of seed development. Using the model plant Arabidopsis thaliana, our studies focus on two types of cytosolic sHSPs, Class I (CI) and Class II(CII). There is total of six Class I (Hsp17.4-I, 17.6A-I, 17.6B-I, 17.6C-I, 17.8-I, and 18.1-I) and two Class II (Hsp17.6-II, Hsp17.7-II) sHSPs in A. thaliana. For CI genes, we are generating mutants using CRISPR methodology in the corresponding genes. At present, we have successfully generated mutants for each individual CI gene along with three double-knock mutant lines for CII sHSPs.  The progress of CII enables us to conduct immuno blot analyses to confirm that these plants are null mutants that do not express CII sHSPs, laying the groundwork for future phenotypic analysis. 

Keywords

Chaperones, Heat Stress, Small Heat Shock Protein

Research Area

Biological Organisms

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