Characterization of squid enolase mRNA: sequence analysis, tissue distribution, and axonal localization.

Abstract:

:Enolase is a glycolytic enzyme whose amino acid sequence is highly conserved across a wide range of animal species. In mammals, enolase is known to be a dimeric protein composed of distinct but closely related subunits: alpha (non-neuronal), beta (muscle-specific), and gamma (neuron-specific). However, little information is available on the primary sequence of enolase in invertebrates. Here we report the isolation of two overlapping cDNA clones and the putative primary structure of the enzyme from the squid (Loligo pealii) nervous system. The composite sequence of those cDNA clones is 1575 bp and contains the entire coding region (1302 bp), as well as 66 and 207 bp of 5' and 3' untranslated sequence, respectively. Cross-species comparison of enolase primary structure reveals that squid enolase shares over 70% sequence identity to vertebrate forms of the enzyme. The greatest degree of sequence similarity was manifest to the alpha isoform of the human homologue. Results of Northern analysis revealed a single 1.6 kb mRNA species, the relative abundance of which differs approximately 10-fold between various tissues. Interestingly, evidence derived from in situ hybridization and polymerase chain reaction experiments indicate that the mRNA encoding enolase is present in the squid giant axon.

journal_name

Neurochem Res

journal_title

Neurochemical research

authors

Chun JT,Gioio AE,Crispino M,Giuditta A,Kaplan BB

doi

10.1007/BF00970738

subject

Has Abstract

pub_date

1995-08-01 00:00:00

pages

923-30

issue

8

eissn

0364-3190

issn

1573-6903

journal_volume

20

pub_type

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