Title Information
Title
Diversification of the SUVH6 Clade of Histone 3 Lysine 9 Methyltransferases in Flowering Plants
Name: Personal
Name Part
Kotak, Jenna Elizabeth
Role
Role Term: Text
creator
Name: Personal
Name Part
Gehring, Mary
Role
Role Term: Text
Reader
Name: Personal
Name Part
Bender, Judith
Role
Role Term: Text
Advisor
Name: Personal
Name Part
Freiman, Richard
Role
Role Term: Text
Reader
Name: Personal
Name Part
Larschan, Erica
Role
Role Term: Text
Reader
Name: Personal
Name Part
Johnson, Mark
Role
Role Term: Text
Reader
Name: Corporate
Name Part
Brown University. Department of Molecular Biology, Cell Biology and Biochemistry
Role
Role Term: Text
sponsor
Origin Information
Copyright Date
2020
Physical Description
Extent
xiii, 179 p.
digitalOrigin
born digital
Note: thesis
Thesis (Ph. D.)--Brown University, 2020
Genre (aat)
theses
Abstract
Transposons are parasitic DNA sequences that pose threats to genome stability across a range of eukaryotes. To defend against transposition into essential genes and destabilizing transposon proliferation, eukaryotes regulate transposon transcription. Gene regulation is often achieved via chromatin modifications of histone proteins and DNA. Through methylation of histone 3 lysine 9 (H3K9), the eukaryotic cell can silence the transcription of transposons as a defense system. This fundamental H3K9 methylation is mediated by H3K9 methyltransferase enzymes that are responsible for efficient and precise modification of silenced regions. While various kingdoms use the same catalytic H3K9 methyltransferase domain, plants have evolved a novel H3K9 methyltransferase class of SUVH proteins. However, why the single SUVH protein present in green algae has expanded and diversified into a large family of proteins in the flowering plant Arabidopsis thaliana is unclear. In this work, I identify unique features of the SUVH6 clade of H3K9 methyltransferases and test the functionalities of these features through a genetic approach. I demonstrate that SUVH6 clade proteins contain longer, likely disordered amino-terminal extensions with a novel motif that function in nuclear localization and activity at preferred loci. My results provide insights into the diversification of chromatin-modifying enzymes and how these enzymes can gain new functions over evolution.
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00859922")
Topic
Chromatin
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01155415")
Topic
Transposons
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00886570")
Topic
DNA--Methylation
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/00917302")
Topic
Evolution (Biology)
Subject (fast) (authorityURI="http://id.worldcat.org/fast", valueURI="http://id.worldcat.org/fast/01065562")
Topic
Plant molecular genetics
Subject
Topic
Histone Modifications
Subject
Topic
Transciptional Regulation
Language
Language Term (ISO639-2B)
English
Record Information
Record Content Source (marcorg)
RPB
Record Creation Date (encoding="iso8601")
20210607
Type of Resource (primo)
dissertations