Investigation Of Protein Interaction Partners Of Plant-Specific Coiled-Coil Proteins

ASU Author/Contributor (non-ASU co-authors, if there are any, appear on document)
Alison R. DeShields (Creator)
Appalachian State University (ASU )
Web Site:
Annkatrin Rose

Abstract: Arabidopsis thaliana Matrix Attachment Region-Binding Filament-Like Protein 1 (AtMFP1) and Filament-like Protein 4-2 (AtFLIP4-2) are unique chloroplast proteins with a coiled-coil protein motif. Coiled-coil domains act as protein-protein interaction domains; thus, AtMFP1 and AtFLIP4-2 may be involved in protein complex formations. Long coiled-coil protein motifs are more common in eukaryotes than prokaryotes and therefore would not be expected in organelles derived from endosymbiosis. However, AtMFP1 is associated with the thylakoid membrane; and AtFLIP4-2 is thought to be located in the chloroplast envelope and could be involved in vesicle transport to form thylakoids. The objective of this research was to further investigate AtMFP1, AtFLIP4-2, and the proteins that interact with AtMFP1 and AtFLIP4-2, and their direct or indirect involvement in photosynthetic processes.

Additional Information

DeShields, A. (2017). Investigation Of Protein Interaction Partners Of Plant-Specific Coiled-Coil Proteins. Unpublished Master’s Thesis. Appalachian State University, Boone, NC.
Language: English
Date: 2017
coiled-coil, protein interaction, Arabidopsis thaliana, MFP1, FLIP4

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