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Novel isoprenylated proteins identified by an expression library screen
B J Biermann1, T A Morehead, S E Tate
1Department of Biology, Indiana University-Purdue University, Indianapolis 46202-5132.
The Journal of Biological Chemistry
|October 14, 1994
Summary
Researchers identified novel isoprenylated proteins in plants using a direct labeling method. This discovery reveals a diverse array of farnesylated proteins in plants, potentially differing from those in other eukaryotes.
Area of Science:
- Molecular Biology
- Biochemistry
- Plant Science
Background:
- Isoprenylated proteins are crucial for eukaryotic cell growth and signal transduction.
- Prenylation involves covalent attachment of isoprenoids to cysteine residues in carboxyl-terminal motifs.
- Current methods have likely left many isoprenylated proteins undiscovered.
Purpose of the Study:
- To identify novel isoprenylated proteins in *Glycine max* (soybean) for further biochemical investigation.
- To explore the diversity of farnesylated proteins in plants.
- To establish a method for discovering post-translationally modified proteins.
Main Methods:
- Screening of a *Glycine max* cDNA expression library using in vitro [3H]farnesyl labeling.
- Identification of proteins with carboxyl-terminal motifs conforming to farnesylation consensus sequences.
- Analysis of novel protein sequences for conserved motifs.
Main Results:
- Successful identification of known and novel farnesylated proteins.
- Discovery of novel proteins containing multiple tandem repeats of a hexapeptide consensus sequence.
- Confirmation of a diverse array of genes encoding farnesylated proteins in plants.
Conclusions:
- Plants possess a wide range of genes for farnesylated proteins.
- Significant differences may exist in farnesylated protein identities between plants and other eukaryotes.
- Direct labeling of expression libraries is an effective strategy for identifying isoprenylated proteins and other post-translationally modified proteins across diverse organisms.