Characterization of the Functional Gene and Several Processed Pseudogenes in the Human Triosephosphate Isomerase Gene Family

Overview

Journal Mol Cell Biol

Specialty Cell Biology

Date 1985 Jul 1

PMID 4022011

Citations 30

Authors

J R Brown

I O Daar

J R Krug

L E Maquat

Affiliations

Soon will be listed here.

Abstract

The functional gene and three intronless pseudogenes for human triosephosphate isomerase were isolated from a recombinant DNA library and characterized in detail. The functional gene spans 3.5 kilobase pairs and is split into seven exons. Its promoter contains putative TATA and CCAAT boxes and is extremely rich in G and C residues (76%). The pseudogenes share a high degree of homology with the functional gene but contain mutations that preclude the synthesis of an active triosephosphate isomerase enzyme. Sequence divergence calculations indicate that these pseudogenes arose approximately 18 million years ago. We present evidence that there is a single functional gene in the human triosephosphate isomerase gene family.

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