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Comparative analysis of BiP gene expression in maize endosperm
R L Wrobel1, G R OBrian, R S Boston
1North Carolina State University, Department of Botany, Raleigh 27695-7612, USA.
Gene
|January 20, 1998
Summary
Researchers identified two maize binding protein (BiP) genes, members of the HSP70 family, expressed in developing kernels. Their expression increased in mutants with abnormal storage proteins and when cells were treated with protein-folding inhibitors.
Area of Science:
- Molecular Biology
- Plant Science
- Genetics
Background:
- Binding protein (BiP) is an endoplasmic reticulum-localized molecular chaperone belonging to the conserved HSP70 family.
- BiP plays a crucial role in protein folding and quality control within the cell.
Purpose of the Study:
- To isolate and characterize maize BiP cDNA clones expressed in immature kernels.
- To investigate the expression patterns and genomic complexity of maize BiP genes, particularly in relation to endosperm development and protein folding stress.
Main Methods:
- Isolation and characterization of BiP cDNA clones from maize.
- RNA gel blot analysis to study gene expression.
- Southern blot analysis to assess genomic complexity.
- Sequence comparison of predicted amino acid sequences.
Main Results:
- Two distinct BiP cDNA clones with high sequence similarity were identified, mapping to unlinked loci in the maize genome.
- Expression of both BiP genes was upregulated in maize mutants (floury-2, Mucronate, Defective endosperm-B30) exhibiting abnormal endosperm storage proteins.
- Increased BiP RNA levels were also observed in cells treated with protein-folding inhibitors (azetidine-2-carboxylic acid and tunicamycin).
- Southern blot analysis indicated the presence of a complex maize BiP multigene family.
Conclusions:
- The BiP genes expressed in maize endosperm are likely coordinately regulated.
- These findings suggest a role for BiP in managing protein folding stress during maize kernel development.
- Maize possesses a complex multigene family for BiP, indicating sophisticated regulation of this chaperone system.