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
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.