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(Received for publication, April 3, 1996, and in revised form, May 23, 1996)
From the Department of Biochemistry and Molecular Biology, Mayo
Clinic Scottsdale, Scottsdale, Arizona 85259
We report the isolation of a novel mouse gene
which encodes a putative hyaluronan synthase. The cDNA was
identified using degenerate reverse transcriptase-polymerase chain
reaction. Degenerate primers were designed based upon an alignment of
the amino acid sequences of Streptococcus pyogenes HasA,
Xenopus laevis DG42, and Rhizobium meliloti
NodC. A mouse embryo cDNA library was screened with the resultant
polymerase chain reaction product, and multiple cDNA clones
spanning 3 kilobase pairs (kb) were isolated. The open reading frame
predicted a 63-kDa protein with several transmembrane sequences,
multiple consensus phosphorylation sites, and four putative hyaluronan
binding motifs. The amino acid sequence displayed 55% identity to
mouse HAS, 56% identity to Xenopus DG42, and 21% identity
to Streptococcus HasA. Northern analysis identified
transcripts of 4.8 kb and 3.2 kb, which were expressed highly in the
developing mouse embryo and at lower levels in adult mouse heart,
brain, spleen, lung, and skeletal muscle. Transfection experiments
demonstrated that mouse Has2 could direct hyaluronan coat biosynthesis
in transfected COS cells, as evidenced by a classical particle
exclusion assay. These results suggest that mammalian HA synthase
activity is regulated by at least two related genes. Accordingly, we
propose the name Has2 for this gene.
Volume 271, Number 38,
Issue of September 20, 1996
pp. 23400-23406
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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