Alternative splicing of repetitive units is responsible for the polydispersities of integumentary mucin B.1 (FIM-B.1) from Xenopus laevis.

Abstract:

:Frog integumentary mucin B.1 (FIM-B.1) represents a polymorphic extracellular mosaic protein which contains tandemly arranged serine/threonine-rich modules as well as cysteine-rich domains. The latter are probably important for oligomerization of FIM-B.1 and have also been found in many proteins of the complement cascade as well as regions homologous to von Willebrand factor. The repetitive modules are targets for extensive O-glycosylation. Previous cDNA cloning experiments clearly established polydispersities within the same individual, which originate from deletions/insertions in the repetitive domain. Here, we analyse part of the corresponding genomic region. Each repetitive unit as well as the cysteine-rich domain is encoded by an individual class 1-1 exon typical of shuffled modules. Alternative splicing of these multiple cassettes creates the polydisperse FIM-B.1 transcripts.

journal_name

Glycoconj J

journal_title

Glycoconjugate journal

authors

Joba W,Hoffmann W

doi

10.1007/BF00702337

subject

Has Abstract

pub_date

1996-10-01 00:00:00

pages

735-40

issue

5

eissn

0282-0080

issn

1573-4986

journal_volume

13

pub_type

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