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Polypeptide structure of germin as deduced from cDNA sequencing.
E Dratewka-Kos1, S Rahman, Z F Grzelczak
1Biochemistry Department, University of Toronto, Ontario, Canada.
The Journal of Biological Chemistry
|March 25, 1989
Summary
Germin synthesis signals wheat embryo growth. This rare glycoprotein
Area of Science:
- Plant molecular biology
- Biochemistry
- Gene regulation
Background:
- Germin, a rare glycoprotein, is synthesized during wheat embryo germination.
- Its synthesis is a key indicator of early plant growth.
- Understanding germin's structure and function provides insights into plant development.
Purpose of the Study:
- To characterize the germin messenger RNA (mRNA) sequence.
- To analyze the deduced amino acid sequence of the mature germin protein.
- To explore potential structural and functional properties of germin.
Main Methods:
- mRNA sequencing and analysis
- Codon usage analysis
- Amino acid sequence analysis
- Homology searches against protein databases
Main Results:
- Germin mRNA is 1075 nucleotides long with distinct 5' and 3' untranslated regions and a coding sequence for a 201-residue mature protein.
- A short distance (9 nucleotides) was observed between a polyadenylation signal and site in the 3' untranslated region.
- The mature protein sequence exhibits an 80% homology with a decapeptide from Escherichia coli glycerol-3-phosphate acyltransferase.
Conclusions:
- Germin's unique mRNA structure and protein sequence suggest specific roles in wheat embryo germination.
- The protein's potential association with membranes and resistance to proteolysis are highlighted.
- Further investigation into germin-gene structure and regulation is warranted for understanding early plant growth.