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Amino acids

Amino acids

Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...

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Inhibition of Aspergillus flavus Growth and Aflatoxin Production in Transgenic Maize Expressing the α-amylase Inhibitor from Lablab purpureus L.

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α-Amylase structural genes in rye.

P Masojć¹, M D Gale

¹Department of Plant Breeding and Biometry, Academy of Agriculture, PL-71-434, Szczecin, Poland.

TAG. Theoretical and Applied Genetics. Theoretische Und Angewandte Genetik

|November 12, 2013

Summary

Researchers investigated rye alpha-amylase (α-Amy) genes using wheat probes. They identified multiple α-Amy1, α-Amy2, and α-Amy3 genes and mapped their locations on rye chromosomes, revealing genetic diversity.

Area of Science:

Plant genetics and molecular biology
Genomics and gene mapping
Biochemistry of enzymes

Background:

Alpha-amylase enzymes are crucial for starch degradation in plants.
Understanding the genetic structure of alpha-amylase genes (α-Amy) in rye (Secale cereale) is important for breeding and functional studies.
Previous studies have indicated the presence of multiple α-Amy gene families in cereals.

Purpose of the Study:

To characterize the copy number and genomic organization of rye α-Amy1, α-Amy2, and α-Amy3 genes.
To map the identified rye α-Amy genes to specific chromosomal locations using restriction fragment length polymorphism (RFLP) markers.
To investigate the genetic diversity and evolutionary relationships of these gene families in rye.

Main Methods:

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Utilized wheat α-amylase cDNA probes for RFLP analysis in crosses between inbred rye lines.

Analyzed segregation patterns in F2 populations to determine gene copy numbers and map gene locations.

Correlated RFLP data with α-amylase isozyme polymorphism analysis.

Main Results:

Identified considerable RFLP polymorphism for α-Amy1 and α-Amy2, suggesting multiple gene copies.
The α-Amy3 region showed higher conservation, with RFLP detected in only one gene.
Estimated three α-Amy1 genes on chromosome 6RL (3cM distance), two or three α-Amy2 genes on chromosome 7RL (5cM distance), and three α-Amy3 genes on chromosome 5RL.

Conclusions:

Rye possesses a complex gene family structure for α-amylase, with distinct copy numbers and chromosomal distributions for α-Amy1, α-Amy2, and α-Amy3.
The study successfully mapped several α-Amy genes relative to RFLP markers on specific rye chromosomes (6RL, 7RL, 5RL).
The findings provide a foundation for further research into the functional roles and evolutionary history of rye α-amylase genes.