Life Sciences Commons^™

The Effects Of Ppal-1 In Arabidopsis Gamete Development, Amanda J White, Susana Perez-Martinez, Mark P. Running

The Cardinal Edge

Prenylation is a type of post-translational modification in which a 15- or 20-carbon lipid is added to the carboxyl (C) terminus of the protein. Arabidopsis thaliana contains the PROTEIN PRENYLTRANSFERASE ALPHA SUBUNIT-LIKE (PPAL) gene, which encodes a protein with homology to the α-subunits of the three known prenylation enzymes, PFT, PGGT, and Rab-GGT. We previously identified two mutations in PPAL, one of which is ppal-1, which contains a T-DNA insertion in the fourth intron. We have previously observed that self-fertilizing heterozygous ppal-1 plants produce progeny in which homozygous ppal-1 is underrepresented. This project attempts to ascertain …

Identification Of The Biological Function Of Rab-Ggt Β-Subunits By Reverse Techniques, Briana L. Seibert, Hyun Jin Jung, Mark P. Running

The Cardinal Edge

Abstract

Protein prenylation is a post-translational process where lipids are added to carboxyl end groups of amino acids, which allows proteins to function properly in the eukaryotic cell. The job of prenylation is to target certain proteins to specific membranes and promote desirable protein-protein interactions. In our study we used reverse genetics techniques to investigate the function of protein prenylation in plant development. To discern the function of protein prenylation, we examined the phenotypic changes caused by specific gene disruptions. In this study the model organism Physcomitrella patens (moss) is utilized due to its simple structure, limited quantities of tissues …

Protein Prenylation In The Moss Physcomitrium Patens, Zayna Qaissi, Anam F. Ahmed, Mark P. Running, Katherine Vo. Brown

The Cardinal Edge

TITLE

Protein Prenylation in the moss Physcomitrium patens

AUTHORS

Zayna H. Qaissi*, Anam F. Ahmed*, Katherine V. Brown, Mark P. Running**

*Co-presenters

**Faculty Mentor

Protein prenylation is the addition of a 15 or 20 carbon lipid to a cysteine near carboxyl terminus of target proteins. Prentlyation increases hydrophobicity, which facilitates membrane associations and protein-protein interaction. Protein prenylation is generally conserved among eukaryotes, and mutations in genes that carry out prenylation are lethal in animals and yeast. In plants prenylation mutations are not always lethal, but they do affect development, disease resistance, biofuel production, and drought response, among other processes of …