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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

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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.

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