Characterization of the mouse liver fructose-1,6-bisphosphatase gene

Abstract

A cDNA encoding fructose-1,6-bisphosphatase (FBPase) was isolated from mouse liver RNA. The cDNA encodes a polypeptide of 338 amino acids (36.9 kDa). The liver and muscle FBPase isoenzymes of the mouse show positional identities of 69% at the cDNA level and 72% at the protein primary structure level. Starting from genomic YAC libraries and based upon the cDNA sequence all functional parts of the mouse liver FBPase gene (including exon-intron boundaries) were PCR-amplified and sequenced. The 5′-flanking regions of the liver and muscle FBPase genes were compared and showed no sequence similarity. Both genes are co-localized at chromosome 13B3-C1. The transcriptional start site was assigned to a guanine 118 bases before the start codon in the liver FBPase gene. An analysis of the steady state mRNA levels of liver and muscle FBPase in various mouse tissues was performed by Northern blotting and RT/PCR.