Identification of Neuronal Isozyme Specific Residues by Comparison of Goldfish Aldolase C to Other Aldolases

• Published in: Comparative biochemistry and physiology. A, Comparative physiology Vol. 117; no. 4; pp. 471 - 476
• Main Authors: Berardini, Tanya Z, Drygas-Williams, Mariola, Callard, Gloria V, Tolan, Dean R
• Format: Journal Article
• Language: English
• Published: United States Elsevier B.V 01.08.1997
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Blotting, Northern; Brain; Brain - enzymology; Carassius auratus; cDNA clone; Cloning, Molecular; Freshwater; Fructose-Bisphosphate Aldolase - chemistry; Goldfish; Isoenzymes; Molecular Sequence Data; Neurons - enzymology; tetraploidization; tissue-specific expression; vertebrate genome evolution; tetraploidization; Brain; goldfish; vertebrate genome evolution; tissue-specific expression; cDNA clone
• ISSN: 0300-9629; 1096-4940
• DOI: 10.1016/S0300-9629(96)00396-9

A 2061 bp cDNA encoding a goldfish ( Carassius auratus) aldolase was isolated from a goldfish brain library. The deduced 362 amino acid sequence is more similar to vertebrate brain (aldolase C) and muscle aldolases (aldolase A) than to the liver isozymes (aldolase B). Northern blot analysis indicates strong expression of the mRNA in brain but not in liver or muscle, which indicates that this is aldolase C rather than aldolase A. Analysis of all known vertebrate aldolase amino acid sequences reveals five residues; Leu-57, Arg-314, Thr-324, Glu-332, and Gly-350 that are present exclusively in aldolase Cs. The goldfish clone possesses all five residues. The residues are primarily located in the carboxyl-terminal region of the enzyme and may play a role in determining the neuronal isozyme-specific properties of the enzyme. Furthermore, the existence of an aldolase C in a teleost fish has implications with respect to the timing of genome duplication events that are thought to have been critical in vertebrate evolution.