Abstract

Transglutaminase 1 (TG1) is an enzyme that is expressed and activated during terminal differentiation of keratinocytes and synthesizes cornified envelope by a cross-linking reaction. The gene encoding human TG1 was isolated from human genomic DNA and characterized. It spans 14.3 kilobase pairs and is composed of 15 exons. All exon-intron junctional sequences conformed to the canonical GT-AG rule. The translation start was located in the second exon. The active site Cys residue of the enzyme was in exon 7. The coding sequence for human TG1 was comprised of 2454 nucleotides identical with the published human TG1-cDNA sequence (Yamanishi, K., Liew, F.-M., Konishi, K., Yasuno, H., Doi, H., Hirano, J., and Fukushima, S. (1991) Biochem. Biophys. Res. Commun. 175, 906-913). The sizes of exons from 3 to 14 were markedly conserved between the genes for the human TG1 and factor XIIIa, another member of the transglutaminase family. The one major and two minor transcription initiation sites of the TG1 gene were determined by primer extension. The 5'-flanking region of the human TG1 gene showed features of a housekeeping gene and contained potential regulatory motifs, including elements found in keratinocyte-related genes. The chromosome sublocalization of the TG1 gene was assigned to 14q11.2.

Highlights

  • Kiyofumi Yamanishi$$, Johji Inazawall, Foo-M Liienw$, Kyoko NonomuraS, Takeshi Ariyamall, Hirokazu Yasuno$, Tatsuo Abell, Hiroshi DoiJlli,ro Hiranoll,and Shoji Fukushimall

  • Transglutaminase 1 (TG1) is an enzyme that is ex- zyme plays a critical role in a specialized biological process pressed and activated during terminal differentiation requiring cross-linking, such as epidermal differentiation, cell of keratinocytes and synthesizes cornified envelopeby aging, apoptosis, hair follicle formation, blood clotting, and a cross-linking reaction.The gene encoding human fertilization

  • The coding sequence for human TG1 was comprised of 2464 nucleotides identical with thepublishedhumanTG1cDNA sequence (Yamanishi,K., Liew, F.-M., Konishi, activity increases as thecells enter the latestage of terminal differentiation [3]

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Summary

Structure of the Gene for Human Transglutaminasel*

Kiyofumi Yamanishi$$, Johji Inazawall, Foo-M Liienw$, Kyoko NonomuraS, Takeshi Ariyamall, Hirokazu Yasuno$, Tatsuo Abell, Hiroshi DoiJlli,ro Hiranoll ,and Shoji Fukushimall. The sizes of exons from 3 to 14 were markedly isolated independentlyin several laboratories [11,12,13,14], and conserved between the genes for the human TG1 and the amino acid sequence of the enzyme has been deduced factor XIIIa, another member of the transglutaminasefrom the nucleotide sequences of the clones. Transglutaminases (EC 2.3.2.13) catalyze acyl transfer reactions between y-carboxamide groups of peptide-bound glutamine residues and the primaryamino groups of various amines, including the €-amino group of lysine in peptides to form t- (y-glutamyl) lysine cross-linking [1, 2] This family of enzymes share thecommon structure of an active site, TyrGly-Gln-Cys-Trp, operated by a cysteine-thiol active center mechanism, and require Caz+in their activation. We assigned the chromosomal localization of the TG1gene to 14q11.2

MATERIALS AND METHODS
RESULTS
Amino acid base pairs
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