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University of Guelph

Distinct C-terminal Amino Acid Sequence Motifs Serve as the Targeting Signals for Outer Mitochondrial Membrane and Plastid Outer Envelope TA Proteins

Abstract

dc:description.abstract

Tail-anchored (TA) proteins are a unique class of functionally diverse membrane proteins that are defined by their single C-terminal transmembrane domain and their ability to insert post-translationally into specific organelles in an Ncytosol-CIMS orientation. While in recent years considerable progress has been made towards understanding the biogenesis of TA proteins in yeast and mammals, relatively little is known about how these proteins are properly partitioned within plant cells, mostly because so few plant TA proteins have been identified. Here we show the results of experiments aimed at cataloguing, in silico, all of the TA outer mitochondrial membrane and plastid outer envelope proteins in Arabidopsis and then identifying and characterising distinct, C-terminal targeting motifs responsible for the proper sorting of at least a subset of these proteins. Collectively, the results of this thesis provide important insight into the molecular mechanisms that underlie the biogenesis of TA proteins in plant cells.

Degree

thesis:*
Grantor dc:publisher
University of Guelph
Year dc:date.issued
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Teresinski, Howard
Advisor dc:contributor.advisor
  • Mullen, Robert

Subjects

dc:subject × 5

Rights

dc:rights
Statement dc:rights
  • Attribution-NonCommercial-NoDerivs 2.5 Canada
Language dc:language.iso
en

Identifiers

dc:identifier.*
Handle dc:identifier.uri
http://hdl.handle.net/10214/8700

Chain of custody

source
Harvested from
University of Guelph
Base URL
atrium.lib.uoguelph.ca/server/oai/request
Last updated
2026-08-21
Source record
OAI-PMH GetRecord
citation

Teresinski, Howard. Distinct C-terminal Amino Acid Sequence Motifs Serve as the Targeting Signals for Outer Mitochondrial Membrane and Plastid Outer Envelope TA Proteins. University of Guelph, 2015. http://hdl.handle.net/10214/8700