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Aldolases a and C are ribonucleolytic components of a neuronal complex that regulates the stability of the light-neurofilament mRNA.

The Journal of neuroscience : the official journal of the Society for Neuroscience

Animals, methods, Blotting, Northern, Blotting, Western, Brain, metabolism, Cell Line, Cercopithecus aethiops, Chromatography, High Pressure Liquid, Cloning, Molecular, Electrophoresis, Gel, Two-Dimensional, Electrophoretic Mobility Shift Assay, Fructose-Bisphosphate Aldolase, physiology, Gene Expression, Gene Expression Regulation, Gene Library, Humans, Immunoprecipitation, Mice, Molecular Sequence Data, Molecular Weight, Neurofilament Proteins, genetics, Peptide Mapping, Protein Biosynthesis, RNA, Messenger, Recombinant Fusion Proteins, Reverse Transcriptase Polymerase Chain Reaction, Transfection

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      A 68 nucleotide segment of the light neurofilament (NF-L) mRNA, spanning the translation termination signal, participates in regulating the stability of the transcript in vivo. Aldolases A and C, but not B, interact specifically with this segment of the transcript in vitro. Aldolases A and C are glycolytic enzymes expressed in neural cells, and their mRNA binding activity represents a novel function of these isozymes. This unsuspected new activity was first uncovered by Northwestern blotting of a brainstem/spinal cord cDNA library. It was confirmed by two-dimensional fractionation of mouse brain cytosol followed by Northwestern hybridization and protein sequencing. Both neuronal aldolases interact specifically with the NF-L but not the heavy neurofilament mRNA, and their binding to the transcript excludes the poly(A)-binding protein (PABP) from the complex. Constitutive ectopic expression of aldolases A and C accelerates the decay of a neurofilament transgene (NF-L) driven by a tetracycline inducible system. In contrast, mutant transgenes lacking mRNA sequence for aldolase binding are stabilized. Our findings strongly suggest that aldolases A and C are regulatory components of a light neurofilament mRNA complex that modulates the stability of NF-L mRNA. This modulation likely involves endonucleolytic cleavage and a competing interaction with the PABP. Interactions of aldolases A and C in NF-L expression may be linked to regulatory pathways that maintain the highly asymmetrical form and function of large neurons.

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