Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase

Citation
H. Ruotsalainen et al., Complete genomic structure of mouse lysyl hydroxylase 2 and lysyl hydroxylase 3/collagen glucosyltransferase, MATRIX BIOL, 20(2), 2001, pp. 137-146
Citations number
31
Categorie Soggetti
Biochemistry & Biophysics
Journal title
MATRIX BIOLOGY
ISSN journal
0945053X → ACNP
Volume
20
Issue
2
Year of publication
2001
Pages
137 - 146
Database
ISI
SICI code
0945-053X(200104)20:2<137:CGSOML>2.0.ZU;2-I
Abstract
Lysyl hydroxylase is an enzyme involved in collagen biosynthesis, catalyzin g the hydroxylation of lysyl residues as a post-translational event. Three isoforms have been characterized so far (LH1, LH2, LH3). Our recent finding s indicate that LH3 possesses, not only lysyl hydroxylase activity, but als o galactosylhydroxylysyl glucosyltransferase activity [Heikkinen et al., J. Biol. Chem. 275 (2000) 36158-36163]. We report here the characterization o f mouse LH2 (Plod2) and LH3/glucosyltransferase (Plod3) genes. Plod2 spans approximately 50 kb of the genomic DNA, and is organized in 20 exons, one o f the exons being alternatively spliced in the RNA processing. Plod3 spans approximately 10 kb of the genomic DNA, and contains 19 exons. Analysis of the 5 ' flanking region with many transcription start sites reveals the lac k of a TATAA box in both genes. Sequence analysis indicated many retroposon -like elements within the Plod3 gene. A comparison was carried out among th e LH1, LH2 and LH3 gene structures characterized so far from different spec ies. (C) 2001 Elsevier Science B.V./International Society of Matrix Biology . All rights reserved.