Complete exon–intron organization of the gene for human lysyl hydroxylase 3 (LH3)

• Published in: Matrix biology Vol. 19; no. 1; pp. 73 - 79
• Main Authors: Rautavuoma, Kati, Passoja, Kaisa, Helaakoski, Tarja, Kivirikko, Kari I.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-02-2000
• Subjects: Amino Acid Sequence; Base Sequence; Binding Sites; Collagen; DNA, Complementary; Exons; Gene structure; Humans; Introns; Lysyl hydroxylase; Molecular Sequence Data; Procollagen-Lysine, 2-Oxoglutarate 5-Dioxygenase - genetics; Promoter Regions, Genetic; Transcription, Genetic; Lysyl hydroxylase; Collagen; Gene structure
• ISSN: 0945-053X; 1569-1802
• DOI: 10.1016/S0945-053X(99)00058-X

Lysyl hydroxylase (LH) catalyzes the formation of hydroxylysine in collagens and related proteins by the hydroxylation of lysine residues in peptide linkages. Three isoenzymes of LH have so far been characterized. We report here that the human LH3 gene is 11.6 kb in size and consists of 19 exons. Transcription is initiated at one major site and several minor sites, the first exon containing 249–335 bp of untranslated sequences and 109 bp of a translated sequence. Exons 2–18 are similar in size to those of the human LH1 gene, whereas the introns are markedly shorter. The LH3 gene contains a total of 15 full length Alu retroposons or partial Alu fragments of more than 100 bp, in introns 5, 6, 12, 15 and 17. These generate a potential for genomic rearrangements, as has been shown for the LH1 gene in Ehlers–Danlos syndrome type VI. The 5′-flanking region of the LH3 gene was found to be entirely different from that of the LH1 gene, suggesting different regulation of these two genes.